Structural and enzymatic characterization of HPO496, a YbgC thioesterase from Helicobacter pylori

被引：21

作者：

Angelini, Alessandro ^{[1
,2
,3
,4
]}

Cendron, Laura ^{[2
,3
,4
]}

Goncalves, Susana ^{[1
]}

Zanotti, Giuseppe ^{[2
,3
,4
]}

Terradot, Laurent ^{[1
]}

机构：

[1] European Synchrotron Radiat Facil, Macromol Crystallog Grp, F-38043 Grenoble, France

[2] Univ Padua, Dept Chem, I-35131 Padua, Italy

[3] ICB CNR, Sect Padua, I-35131 Padua, Italy

[4] Venetian Inst Mol Med, I-35127 Padua, Italy

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2008年 / 72卷 / 04期

关键词：

acyl-CoA; bacterial membrane; Tol-Pal system; lipid biogenesis; hot-dog fold;

D O I：

10.1002/prot.22014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

YbgC proteins are bacterial acyl-CoA thioesterases associated with the Tol-Pal system. This system is important for cell envelope integrity and is part of the cell division machinery. In E. coli, YbgC associates with the cell membrane and is part of a protein network involved in lipid biogenesis. In the human pathogen Helicobacter pylori, a putative homologue of YbgC, named HP0496, was found to interact with the cytotoxin CagA by two different studies. We have determined its crystal structure and characterized its enzymatic activity. The structure of HP0496 shows that it is a member of the hot-dog family of proteins, with a epsilon gamma tetrameric arrangement. Finally, enzymatic assays performed with the purified protein showed that HP0496 is an acyl-CoA thioesterase that favors long-chain substrates.

引用

页码：1212 / 1221

页数：10

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