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Science 17 August 2007:
Vol. 317. no. 5840, pp. 961 - 964
DOI: 10.1126/science.1143993
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Reports

Structure and Function of an Essential Component of the Outer Membrane Protein Assembly Machine

Seokhee Kim,1 Juliana C. Malinverni,2 Piotr Sliz,3,4 Thomas J. Silhavy,2 Stephen C. Harrison,3,4 Daniel Kahne1,3*

Integral ß-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 ß-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.

1 Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
2 Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
3 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
4 Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine, Boston, MA 02115, USA.

* To whom correspondence should be addressed. E-mail: kahne{at}chemistry.harvard.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)