Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter

Science

Volumn 322, Issue 5902, 2008, Pages 709-713

  Weyand, Simone ^a,b,c   Shimamura, Tatsuro ^b,c,d   Yajima, Shunsuke ^b,c,h   Suzuki, ShuN'Ichi ^e,i   Mirza, Osman ^b,j   Krusong, Kuakarun ^b,k   Carpenter, Elisabeth P ^a,b   Rutherford, Nicholas G ^e   Hadden, Jonathan M ^e   O'Reilly, John ^e   Ma, Pikyee ^e   Saidijam, Massoud ^e,f   Patching, Simon G ^e   Hope, Ryan J ^e   Norbertczak, Halina T ^e   Roach, Peter C J ^e   Iwata, So ^a,b,c,d,g   Henderson, Peter J F ^e   Cameron, Alexander D ^a,b,c  

^a DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d KYOTO UNIVERSITY   (Japan)

^e UNIVERSITY OF LEEDS   (United Kingdom)

^f HAMADAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^g RIKEN   (Japan)

^h TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

ⁱ AJINOMOTO CO INC   (Japan)

^j UNIVERSITY OF COPENHAGEN   (Denmark)

^k CHULALONGKORN UNIVERSITY   (Thailand)

more..

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CATION; MEMBRANE PROTEIN; NUCLEOBASE TRANSPORTER; PROTEIN MHP1; UNCLASSIFIED DRUG;

BACTERIUM; CARBOHYDRATE; METABOLITE; MOLECULAR ANALYSIS; NUCLEIC ACID; SUBSTRATE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; MEMBRANE TRANSPORT; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; STRUCTURE ANALYSIS;

ACTINOMYCETALES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CATIONS; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; HYDANTOINS; ION TRANSPORT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEOBASE TRANSPORT PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SODIUM; SYMPORTERS;

MICROBACTERIUM LIQUEFACIENS;

EID: 55349092991     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1164440     Document Type: Article

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40. This research was funded primarily by the Biotechnology and Biological Sciences Research Council (grant nos. B17935 and BB/C51725), with important contributions from Ajinomoto Incorporated, the European Membrane Protein consortium (grant no. LSHG-CT-2004-504601), the Membrane Protein Structure Initiative (grant no. BBS/B/14418), and the Wellcome Trust (grant no. 062164/Z/00/Z). We wish to thank the Membrane Protein Laboratory (MPL) at the Diamond Light Source Limited for use of the MPL facilities. J. Abramson kindly provided us with the coordinates of vSGLT before their release from the Protein Data Bank (PDB). We are also grateful to S. Phillips, S. Baldwin, P. Gilmartin, S. Radford, D. Drew, M. Jormakka, K. Watanabe, and M. Iwata for support or advice. The Japan Society for the Promotion of Science provided personal funding to S.Y. and the Leverhulme Trust to P.J.F.H. S.W. was a recipient of a European Molecular Biology Organization long-term fellowship. The coordinates and the structure factors for Mhp1 without substrate and the hydantoin complex have been deposited in the PDB (entries 2JLN and 2JLO, respectively).