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J. Biol. Chem., Vol. 283, Issue 8, 5208-5216, February 22, 2008

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Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC^*

From the Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada

The essential bacterial membrane protein YidC facilitates insertion and assembly of proteins destined for integration into the inner membrane. It has homologues in both mitochondria and chloroplasts. Here we report the crystal structure of the Escherichia coli YidC major periplasmic domain (YidC_ECP1) at 2.5Å resolution. This domain is present in YidC from Gram-negative bacteria and is more than half the size of the full-length protein. The structure reveals that YidC_ECP1 is made up of a large twisted β-sandwich protein fold with a C-terminal -helix that packs against one face of the β-sandwich. Our structure and sequence analysis reveals that the C-terminal -helix and the β-sheet that it lays against are the most conserved regions of the domain. The region corresponding to the C-terminal -helix was previously shown to be important for the protein insertase function of YidC and is conserved in other YidC-like proteins. The structure reveals that a region of YidC that was previously shown to be involved in binding to SecF maps to one edge of the β-sandwich. Electrostatic analysis of the molecular surface for this region of YidC reveals a predominantly charged surface and suggests that the SecF-YidC interaction may be electrostatic in nature. Interestingly, YidC_ECP1 has significant structural similarity to galactose mutarotase from Lactococcus lactis, suggesting that this domain may have another function besides its role in membrane protein assembly.

Received for publication, October 30, 2007 , and in revised form, December 12, 2007.

The atomic coordinates and structure factors (code 3BLC) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by a Canadian Institute of Health Research operating grant, a National Science and Engineering Research Council of Canada discovery grant, a Michael Smith Foundation for Health Research Senior Scholar award, a Canadian Foundation of Innovation grant (to M. P.), and a Michael Smith Foundation for Health Research postdoctoral fellow award (to D. C. O.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Simon Fraser University, Dept. of Molecular Biology and Biochemistry, South Science Bldg., 8888 University Dr., Burnaby, British Columbia V5A 1S6, Canada. Tel.: 604-291-4320; Fax: 604-291-5583; E-mail: mpaetzel{at}sfu.ca.

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This article has been cited by other articles:

				S. Ravaud, G. Stjepanovic, K. Wild, and I. Sinning The Crystal Structure of the Periplasmic Domain of the Escherichia coli Membrane Protein Insertase YidC Contains a Substrate Binding Cleft J. Biol. Chem., April 4, 2008; 283(14): 9350 - 9358. [Abstract] [Full Text] [PDF]