Structure and function of an essential component of the outer membrane protein assembly machine

被引：296

作者：

Kim, Seokhee

Malinverni, Juliana C.

Sliz, Piotr

Silhavy, Thomas J.

Harrison, Stephen C.

Kahne, Daniel ^{[1
]}

机构：

[1] Harvard Univ, Dept Chem & Chem Biol, Cambridge, MA 02138 USA

[2] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA

[3] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[4] Howard Hughes Med Inst, Boston, MA 02115 USA

[5] Childrens Hosp, Mol Med Lab, Boston, MA 02115 USA

来源：

SCIENCE | 2007年 / 317卷 / 5840期

关键词：

D O I：

10.1126/science.1143993

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Integral beta-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.

引用

收藏

页码：961 / 964

页数：4

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