5D7B

Trigonal Crystal Structure of an acetylester hydrolase from Corynebacterium glutamicum

5D7B の概要

• エントリーDOI: 10.2210/pdb5d7b/pdb
• 関連するPDBエントリー: 5D60
• 分子名称: Homoserine O-acetyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: acetylester hydrolase, alpha/beta-hydrolase, hydrolase
• 由来する生物種: Corynebacterium glutamicum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79121.82

構造登録者

Niefind, K.,Toelzer, C.,Pal, S.,Altenbuchner, J.,Watzlawick, H. (登録日: 2015-08-13, 公開日: 2015-12-16, 最終更新日: 2024-01-10)

主引用文献

Tolzer, C.,Pal, S.,Watzlawick, H.,Altenbuchner, J.,Niefind, K.
A novel esterase subfamily with alpha / beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to l-homoserine O-acetyl transferases.
Febs Lett., 590:174-184, 2016

PubMed Abstract: MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of α/β-hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x-ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl-CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.

PubMed: 26787467
DOI: 10.1002/1873-3468.12031

実験手法

X-RAY DIFFRACTION (3.2 Å)