Mechanism of substrate recognition and transport by an amino acid antiporter

Xiang Gao, Lijun Zhou, Xuyao Jiao, Feiran Lu, Chuangye Yan, Xin Zeng, Jiawei Wang and Yigong Shi ()
Additional contact information
Xiang Gao: Ministry of Education Protein Science Laboratory,
Lijun Zhou: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Xuyao Jiao: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Feiran Lu: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Chuangye Yan: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Xin Zeng: Ministry of Education Protein Science Laboratory,
Jiawei Wang: State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
Yigong Shi: Ministry of Education Protein Science Laboratory,

Nature, 2010, vol. 463, issue 7282, 828-832

Abstract: Amino acid antiporter recognition mechanisms Some bacteria rely on the amino acid antiporter AdiC to expel protons by exchanging intracellular agmatine for extracellular arginine. The structure of the substrate-free form of AdiC is known, and it is believed to represent an 'outward-open' conformation. In this study, Gao et al. solved the X-ray crystal structure of an AdiC variant bound to Arg. The positively charged Arg is enclosed in an acidic binding chamber, with the head groups of Arg hydrogen bonded to main chain atoms of AdiC and the aliphatic portion of Arg stacked by hydrophobic side chains of highly conserved residues. The authors identified three potential gates, involving four aromatic residues and Glu 208, which may work in concert to differentially regulate the upload and release of Arg and Agm.

Date: 2010
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature08741 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:463:y:2010:i:7282:d:10.1038_nature08741

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature08741

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().