TY - JOUR
T1 - Structure and function of an essential component of the outer membrane protein assembly machine
AU - Kim, Seokhee
AU - Malinverni, Juliana C.
AU - Sliz, Piotr
AU - Silhavy, Thomas J.
AU - Harrison, Stephen C.
AU - Kahne, Daniel
N1 - Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/8/17
Y1 - 2007/8/17
N2 - Integral β-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 β-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.
AB - Integral β-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 β-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.
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U2 - 10.1126/science.1143993
DO - 10.1126/science.1143993
M3 - Article
C2 - 17702946
AN - SCOPUS:34548139422
SN - 0036-8075
VL - 317
SP - 961
EP - 964
JO - Science
JF - Science
IS - 5840
ER -