Crystal structure of the potassium channel KirBac1.1 in the closed state

Science

Volumn 300, Issue 5627, 2003, Pages 1922-1926

  Kuo, Anling ^a   Gulbis, Jacqueline M ^b   Antcliff, Jennifer F ^a   Rahman, Tahmina ^a   Lowe, Edward D ^a   Zimmer, Jochen ^a   Cuthbertson, Jonathan ^a   Ashcroft, Frances M ^a   Ezaki, Takayuki ^c   Doyle, Declan A ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^c GIFU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CRYSTAL STRUCTURE;

PROKARYOTES;

POTASSIUM;

INWARDLY RECTIFYING POTASSIUM CHANNEL; MAGNESIUM ION; MEMBRANE PROTEIN; PROTEIN KIRBAC1.1; RUBIDIUM CHLORIDE; THIOMERSAL; UNCLASSIFIED DRUG;

CRYSTAL STRUCTURE; POTASSIUM;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROKARYOTE; PROTEIN CONFORMATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; BURKHOLDERIA PSEUDOMALLEI; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HYDROPHOBICITY; ION CHANNEL GATING; ION TRANSPORT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POTASSIUM; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

PROKARYOTA;

EID: 12444274301     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1085028     Document Type: Article

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30. We thank the staff of the European Synchrotron Radiation Facility for help with data collection, including E. Gordon, J. McCarthy, S. Monaco, and S. Kozieiski. D.A.D. is grateful for support and helpful discussions from L. Johnson, M. Sansom, B. Guy, B. Wallace, L. Hong S. Iwata, and M. Noble. J.M.G. thanks P. Colman and B. Smith. F.M.A. is funded by the Wellcome Trust and Medical Research Council. J.M.G. was funded by an International Senior Fellowship of the Wellcome Trust and by Australian National Health and Medical Research Council grant 257528. This work was funded by a Wellcome Trust Research Career Development Fellowship awarded to D.A.D. Coordinates for the KirBac1.1 structure have been deposited with the Protein Data Bank (accession code 1P7B; ID no. RCSB019097).