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
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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