3NEV

Crystal structure of YagE, a prophage protein from E. coli K12 in complex with KDGal

3NEV の概要

• エントリーDOI: 10.2210/pdb3nev/pdb
• 関連するPDBエントリー: 2V8Z 2V9D 3N2X
• 分子名称: Uncharacterized protein yagE, 1,2-ETHANEDIOL, 3-DEOXY-D-LYXO-HEXONIC ACID, ... (4 entities in total)
• 機能のキーワード: tim barrel, protein-ligand complex, aldolase, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129696.27

構造登録者

Bhaskar, V.,Kumar, P.M.,Manicka, S.,Krishnaswamy, S. (登録日: 2010-06-09, 公開日: 2011-04-13, 最終更新日: 2024-11-20)

主引用文献

Bhaskar, V.,Kumar, M.,Manicka, S.,Tripathi, S.,Venkatraman, A.,Krishnaswamy, S.
Identification of biochemical and putative biological role of a xenolog from Escherichia coli using structural analysis.
Proteins, 79:1132-1142, 2011

PubMed Abstract: YagE is a 33 kDa prophage protein encoded by CP4-6 prophage element in Escherichia coli K12 genome. Here, we report the structures of YagE complexes with pyruvate (PDB Id 3N2X) and KDGal (2-keto-3-deoxy galactonate) (PDB Id 3NEV) at 2.2A resolution. Pyruvate depletion assay in presence of glyceraldehyde shows that YagE catalyses the aldol condensation of pyruvate and glyceraldehyde. Our results indicate that the biochemical function of YagE is that of a 2-keto-3-deoxy gluconate (KDG) aldolase. Interestingly, E. coli K12 genome lacks an intrinsic KDG aldolase. Moreover, the over-expression of YagE increases cell viability in the presence of certain bactericidal antibiotics, indicating a putative biological role of YagE as a prophage encoded virulence factor enabling the survival of bacteria in the presence of certain antibiotics. The analysis implies a possible mechanism of antibiotic resistance conferred by the over-expression of prophage encoded YagE to E. coli.

PubMed: 21294156
DOI: 10.1002/prot.22949

実験手法

X-RAY DIFFRACTION (2.19 Å)