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Crystal structure of Gig2 protein from Candida albicans provides a structural insight into DUF1479 family oxygenases

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Bibliographic Details
Title: Crystal structure of Gig2 protein from Candida albicans provides a structural insight into DUF1479 family oxygenases
Authors: Rani, Priya, Gautam, Gunjan, Anwar, Tamanna, Gourinath, Samudrala, Datta, Asis
Source: International Journal of Biological Macromolecules. 150:1272-1280
Publisher Information: Elsevier BV, 2020.
Publication Year: 2020
Subject Terms: Fungal Proteins/chemistry, 0301 basic medicine, Protein Structure, Secondary, Iron, Crystallography, X-Ray, Ligands, Protein Structure, Secondary, Acetylglucosamine, Fungal Proteins, 03 medical and health sciences, Metals/chemistry, Protein Domains, Catalytic Domain, Candida albicans, Escherichia coli, 0303 health sciences, Acetylglucosamine/chemistry, Crystallography, Ketoglutaric Acids/chemistry, Virulence, Candida albicans/enzymology, Oxidative Stress, Iron/chemistry, Metals, Escherichia coli/metabolism, X-Ray, Oxygenases, Ketoglutaric Acids, Oxygenases/chemistry, Protein Binding
Description: Candida albicans, GlcNAc inducible gene 2 (Gig2) is important for its virulence, oxidative stress adaptation and is supposed to be a part of the undefined GlcNAc metabolic network. On the basis of sequence homology, Gig2 is classified as a putative oxidoreductase of DUF1479 family (Domain of Unknown Function) with no reported structure and function. In this work, we have elucidated the crystal structure of Gig2 protein using X-ray crystallography at 1.7 A resolution. Crystals were improved using successive macro-seeding technique. Structure was solved by molecular replacement using a template (PDBID: 2CSG) with a mere 27% identity with Gig2, followed by manual and automated model building. Gig2 exists as a monomer with a single large DUF1479 domain and is composed of a cupin like double stranded β-helix (DBSH) core fold with Iron (Fe) in the active site. This is the first report of DUF1479 family proteins which identifies and highlights its unique structural features. Crystal structure elucidation, structural comparisons, and docking studies proposes Gig2 as a non-heme Fe (II) containing 2-oxoglutarate dependent oxygenase.
Document Type: Article
Language: English
ISSN: 0141-8130
DOI: 10.1016/j.ijbiomac.2019.10.138
Access URL: https://pubmed.ncbi.nlm.nih.gov/31743702
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=202002287130786512
https://pubmed.ncbi.nlm.nih.gov/31743702/
https://www.sciencedirect.com/science/article/pii/S0141813019340863
https://www.ncbi.nlm.nih.gov/pubmed/31743702
https://pubag.nal.usda.gov/catalog/6766286
Rights: Elsevier TDM
Accession Number: edsair.doi.dedup.....2d2683f18b95b24fb322be8a31a2378d
Database: OpenAIRE
Description
Abstract:Candida albicans, GlcNAc inducible gene 2 (Gig2) is important for its virulence, oxidative stress adaptation and is supposed to be a part of the undefined GlcNAc metabolic network. On the basis of sequence homology, Gig2 is classified as a putative oxidoreductase of DUF1479 family (Domain of Unknown Function) with no reported structure and function. In this work, we have elucidated the crystal structure of Gig2 protein using X-ray crystallography at 1.7 A resolution. Crystals were improved using successive macro-seeding technique. Structure was solved by molecular replacement using a template (PDBID: 2CSG) with a mere 27% identity with Gig2, followed by manual and automated model building. Gig2 exists as a monomer with a single large DUF1479 domain and is composed of a cupin like double stranded β-helix (DBSH) core fold with Iron (Fe) in the active site. This is the first report of DUF1479 family proteins which identifies and highlights its unique structural features. Crystal structure elucidation, structural comparisons, and docking studies proposes Gig2 as a non-heme Fe (II) containing 2-oxoglutarate dependent oxygenase.
ISSN:01418130
DOI:10.1016/j.ijbiomac.2019.10.138