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Homology-Modeled Structure of the Yeast Mitochondrial Citrate Transport Protein

Department of Biochemistry and Molecular Biology, Rosalind Franklin University of Medicine and Science, North Chicago, Illinois 60064

Correspondence: Address reprint requests to: D. Eric Walters, Professor of Biochemistry and Molecular Biology, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Rd., North Chicago, IL 60064. Tel.: 847-578-8613; Fax: 847-578-3240; E-mail: eric.walters{at}finchcms.edu.

We have used homology modeling to construct a three-dimensional model of the yeast mitochondrial citrate transport protein (CTP), based on the recently published x-ray crystal structure of another mitochondrial transport protein, the ADP/ATP carrier. Superposition of the backbone traces of the homology-modeled CTP onto the crystallographically determined ADP carrier structure indicates that the CTP transmembrane domains are well modeled (i.e., root mean square deviation of 0.94 Å), whereas the loops facing the intermembrane space and the mitochondrial matrix are less certain (i.e., root mean square deviation values of 0.72–2.06 Å). The homology-modeled CTP is consistent with our earlier de novo models of the transporter's transmembrane domains, with respect to residues which face into the transport path. Importantly, the resulting model is consistent with our previous experimental data obtained from measuring reactivity of 34 single cysteine mutants in transmembrane domains 3 and 4 with methanethiosulfonate reagents. The model also points to a likely dimer interface region. In conclusion, our data help to define the substrate translocation pathway in both the modeled CTP structure and the crystallographic ADP carrier structure.

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				C. Ma, R. Kotaria, J. A. Mayor, S. Remani, D. E. Walters, and R. S. Kaplan The Yeast Mitochondrial Citrate Transport Protein: CHARACTERIZATION OF TRANSMEMBRANE DOMAIN III RESIDUE INVOLVEMENT IN SUBSTRATE TRANSLOCATION J. Biol. Chem., January 21, 2005; 280(3): 2331 - 2340. [Abstract] [Full Text] [PDF]