Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1

Science

Volumn 328, Issue 5977, 2010, Pages 470-473

  Shimamura, Tatsuro ^a,b,c   Weyand, Simone ^a,b,d   Beckstein, Oliver ^e   Rutherford, Nicholas G ^f   Hadden, Jonathan M ^f   Sharpies, David ^f   Sansom, Mark S P ^e   Iwata, So ^a,b,c,d,g   Henderson, Peter J F ^f   Cameron, Alexander D ^a,b,c,d  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c KYOTO UNIVERSITY   (Japan)

^d Diamond Light Source   (United Kingdom)

^e UNIVERSITY OF OXFORD   (United Kingdom)

^f UNIVERSITY OF LEEDS   (United Kingdom)

^g RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYDANTOIN DERIVATIVE; MHP1 PROTEIN; SODIUM; UNCLASSIFIED DRUG;

BACTERIUM; BIOCHEMISTRY; CRYSTAL STRUCTURE; MOLECULAR ANALYSIS; PROTEIN;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; MEMBRANE TRANSPORT; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; SIMULATION;

ACTINOMYCETALES; AMINO ACID MOTIFS; BACTERIAL PROTEINS; BINDING SITES; BIOLOGICAL TRANSPORT; CRYSTALLOGRAPHY, X-RAY; HYDANTOINS; ION TRANSPORT; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SODIUM;

MICROBACTERIUM LIQUEFACIENS;

EID: 77951585158     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1186303     Document Type: Article

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32. This work was funded by the Biotechnology and Biological Sciences Research Council (BBSRC) (grant no. BB/C51725) and the European Union (EMeP grant, LSHGCT-2004-504601, and EDIG grant 201924). The authors are grateful for the use of the Membrane Protein Laboratory funded by the Wellcome Trust (grant 062164/ Z/00/Z) at the Diamond Light Source Limited. P.J.F.H. received personal funding from the Leverhulme Trust, S.W. from a European Molecular Biology Organization long-term fellowship, T.S. from a Grant-in-Aid for Scientific Research (B) (grant 21370043) and J.H. from the BBSRC MPSi (grant BBS/B/14418). We appreciate the additional support of S. Suzuki and Ajinomoto Company Incorporated. A part of this work was also supported by a grant from the ERATO IWATA Human Receptor Crystallography Project from the Japan Science and Technology Agency and by the Targeted Proteins Research Program of MEXT, Japan. Data were collected at the European Synchrotron Radiation Facility, and further experiments were carried out at Diamond Light Source. We are grateful to D. Drew for critical reading of the manuscript. The coordinates and the structure factors for Mhp1 have been deposited in the Protein Data Bank (entry 2×79).