Dimerization allows DNA target site recognition by the NarL response regulator

Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition...

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Vydané v:	Nature Structural Biology Ročník 9; číslo 10; s. 771 - 778
Hlavní autori:	Maris, Ann E., Sawaya, Michael R., Kaczor-Grzeskowiak, Maria, Jarvis, Michael R., Bearson, Shawn M.D., Kopka, Mary L., Schröder, Imke, Gunsalus, Robert P., Dickerson, Richard E.
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	New York Nature Publishing Group US 01.10.2002 Nature Publishing Group
Predmet:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biochemistry Biological Microscopy Biomedical and Life Sciences Cloning, Molecular Crystallography, X-Ray Deoxyribonucleic acid Dimerization DNA DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism E coli Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Life Sciences Membrane Biology Nucleic Acid Conformation Promoter Regions, Genetic Protein Binding Protein Conformation Protein Structure Protein Structure, Secondary Recombinant Proteins - chemistry Structure-Activity Relationship
ISSN:	1072-8368, 1545-9993, 1545-9985
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Shrnutí:	Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component response regulators can bind DNA. DNA recognition is accompanied by the formation of a new dimerization interface, which could occur only in the full-length protein via a large intramolecular domain rearrangement. The DNA is recognized by the concerted effects of solvation, van der Waals forces and inherent DNA deformability, rather than determined primarily by major groove hydrogen bonding. These subtle forces permit a small DNA-binding domain to perturb the DNA helix, leading to major DNA curvature and a transition from B- to A-form DNA at the binding site, where valine on the recognition helix interacts unexpectedly with the polar major groove floor.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 14 ObjectType-Article-2 ObjectType-Feature-1 content type line 23 ObjectType-Feature-2
ISSN:	1072-8368 1545-9993 1545-9985
DOI:	10.1038/nsb845