Crystal structure of human gamma-butyrobetaine hydroxylase

► Crystal structure of gamma-butyrobetaine hydroxylase solved at 2 Å resoluttion. ► Novel dimerization interface among 2-ketoglutarate oxygenases. ► Unique N-terminal Zn-containing domain. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthes...

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Published in:	Biochemical and biophysical research communications Vol. 398; no. 4; pp. 634 - 639
Main Authors:	Tars, Kaspars, Rumnieks, Janis, Zeltins, Andris, Kazaks, Andris, Kotelovica, Svetlana, Leonciks, Ainars, Sharipo, Jelena, Viksna, Arturs, Kuka, Janis, Liepinsh, Edgars, Dambrova, Maija
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 06.08.2010
Subjects:	2-Ketoglutarate Carnitine Catalytic Domain Crystal structure Crystallography Dioxygenase Drug Design Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology gamma-Butyrobetaine Dioxygenase - antagonists & inhibitors gamma-Butyrobetaine Dioxygenase - chemistry gamma-Butyrobetaine Dioxygenase - genetics Gamma-buyrobetaine hydroxylase Humans Methylhydrazines - pharmacology Mildronate Protein Multimerization Recombinant Proteins - chemistry Recombinant Proteins - genetics Zinc - chemistry GBBH Dioxygenase 2-Ketoglutarate GBB Gamma-buyrobetaine hydroxylase Mildronate DBSH 2KG Carnitine
ISSN:	0006-291X, 1090-2104, 1090-2104
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Abstract	► Crystal structure of gamma-butyrobetaine hydroxylase solved at 2 Å resoluttion. ► Novel dimerization interface among 2-ketoglutarate oxygenases. ► Unique N-terminal Zn-containing domain. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0 Å resolution. The GBBH monomer consists of a catalytic double-stranded β-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His–X–Asp–X n –His triad, which is found in all related enzymes.
AbstractList	a-[ordm Crystal structure of gamma-butyrobetaine hydroxylase solved at 2aa resoluttion. a-[ordm Novel dimerization interface among 2-ketoglutarate oxygenases. a-[ordm Unique N-terminal Zn-containing domain. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0aa resolution. The GBBH monomer consists of a catalytic double-stranded b-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His-X-Asp-X n -His triad, which is found in all related enzymes. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His-X-Asp-X(n)-His triad, which is found in all related enzymes.Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His-X-Asp-X(n)-His triad, which is found in all related enzymes. ► Crystal structure of gamma-butyrobetaine hydroxylase solved at 2 Å resoluttion. ► Novel dimerization interface among 2-ketoglutarate oxygenases. ► Unique N-terminal Zn-containing domain. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0 Å resolution. The GBBH monomer consists of a catalytic double-stranded β-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His–X–Asp–X n –His triad, which is found in all related enzymes. Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domain, which is found in all 2KG oxygenases, and a smaller N-terminal domain. Extensive interactions between two monomers confirm earlier observations that GBBH is dimeric in its biological state. Although many 2KG oxygenases are multimeric, the dimerization interface of GBBH is very different from that of related enzymes. The N-terminal domain of GBBH has a similar fold to the DUF971 superfamily, which consists of several short bacterial proteins with unknown function. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. Although several other 2KG oxygenases with known structures have more than one domain, none of them resemble the N-terminal domain of GBBH. The N-terminal domain may facilitate dimer formation, but its precise biological role remains to be discovered. The active site of the catalytic domain of GBBH is similar to that of other 2KG oxygenases, and Fe(II)-binding residues form a conserved His-X-Asp-X(n)-His triad, which is found in all related enzymes.
Author	Sharipo, Jelena Kotelovica, Svetlana Leonciks, Ainars Zeltins, Andris Tars, Kaspars Kuka, Janis Liepinsh, Edgars Kazaks, Andris Viksna, Arturs Rumnieks, Janis Dambrova, Maija
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Copyright	2010 Elsevier Inc. Copyright (c) 2010 Elsevier Inc. All rights reserved. Copyright (c) 2010 Elsevier Inc. All rights reserved.
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Keywords	GBBH Dioxygenase 2-Ketoglutarate GBB Gamma-buyrobetaine hydroxylase Mildronate DBSH 2KG Carnitine
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Snippet	► Crystal structure of gamma-butyrobetaine hydroxylase solved at 2 Å resoluttion. ► Novel dimerization interface among 2-ketoglutarate oxygenases. ► Unique... Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of... a-[ordm Crystal structure of gamma-butyrobetaine hydroxylase solved at 2aa resoluttion. a-[ordm Novel dimerization interface among 2-ketoglutarate oxygenases....
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SubjectTerms	2-Ketoglutarate Carnitine Catalytic Domain Crystal structure Crystallography Dioxygenase Drug Design Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology gamma-Butyrobetaine Dioxygenase - antagonists & inhibitors gamma-Butyrobetaine Dioxygenase - chemistry gamma-Butyrobetaine Dioxygenase - genetics Gamma-buyrobetaine hydroxylase Humans Methylhydrazines - pharmacology Mildronate Protein Multimerization Recombinant Proteins - chemistry Recombinant Proteins - genetics Zinc - chemistry
Title	Crystal structure of human gamma-butyrobetaine hydroxylase
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