Structure of the light-driven chloride pump halorhodopsin at 1.8 Å Resolution

Science

Volumn 288, Issue 5470, 2000, Pages 1390-1396

  Kolbe, Michael ^a   Besir, Hüseyin ^a   Essen, Lars Oliver ^a   Oesterhelt, Dieter ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HALORHODOPSIN; MEMBRANE PROTEIN; PALMITIC ACID; SCHIFF BASE;

ANION TRANSPORT; ARTICLE; BINDING AFFINITY; CALCULATION; CHLORIDE PUMP; CHROMATOPHORE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; MEMBRANE TRANSPORT; PRIORITY JOURNAL; PROTON TRANSPORT;

BACTERIORHODOPSINS; BINDING SITES; BIOLOGICAL TRANSPORT, ACTIVE; CELL MEMBRANE; CHLORIDES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; ELECTROSTATICS; HALOBACTERIUM SALINARUM; HALORHODOPSINS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; ION PUMPS; ION TRANSPORT; LIGHT; LIPIDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTONS; SCHIFF BASES; THERMODYNAMICS;

ARCHAEA;

EID: 0034717007     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.288.5470.1390     Document Type: Article

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50. The authors are very grateful for support by H. Bartunik at synchrotron beamline BW6, Max-Planck groups for structural molecular biology, Hamburg, W. Burmeister at ID14-3, European Synchrotron Radiation Facility Grenoble, and J. Tittor for discussion and DNA sequencing. This work was supported by EU grant BIO4-CT98-0415, Sonderfarschungsbereich 533 (Deutsche Forschungsgemeinschaft), and the Fonds der Chemischen Industrie. Coordinates and structure factors are available from the Protein Data Bank (accession number 1E12).