Structure of a prokaryotic virtual proton pump at 3.2 Å resolution

Yiling Fang, Hariharan Jayaram, Tania Shane, Ludmila Kolmakova-Partensky, Fang Wu, Carole Williams, Yong Xiong and Christopher Miller ()
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Yiling Fang: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Hariharan Jayaram: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Tania Shane: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Ludmila Kolmakova-Partensky: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Fang Wu: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Carole Williams: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA
Yong Xiong: Yale University, New Haven, Connecticut 06520, USA
Christopher Miller: Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA

Nature, 2009, vol. 460, issue 7258, 1040-1043

Abstract: The AdiC proton pump Little is known about the structure of the APC superfamily of membrane proteins, which transport amino acids, polyamines and cations in a variety of physiological contexts. Here, Fang et al. report the 3.2 Å crystal structure of AdiC, an arginine–agmatine antiporter from Escherichia coli. The protein, which is captured in a substrate-free outward-facing conformation, has the same structural fold as a number of Na+-coupled transporter families. Fang et al. also demonstrate that each subunit of AdiC functions independently.

Date: 2009
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DOI: 10.1038/nature08201

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