1C8S

BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE

Summary for 1C8S

• Entry DOI: 10.2210/pdb1c8s/pdb
• Related: 1C3W
• Descriptor: BACTERIORHODOPSIN ("M" STATE INTERMEDIATE), 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, 2,10,23-TRIMETHYL-TETRACOSANE, ... (5 entities in total)
• Functional Keywords: ion pump, membrane protein, retinal protein, lipids, photoreceptor, haloarchaea, d96n m intermediate, ion transport, merohedral twinning
• Biological source: Halobacterium salinarum
• Cellular location: Cell membrane; Multi-pass membrane protein: P02945
• Total number of polymer chains: 1
• Total formula weight: 29064.91

Authors

Luecke, H. (deposition date: 1999-07-29, release date: 1999-10-20, Last modification date: 2024-10-16)

Primary citation

Luecke, H.,Schobert, B.,Richter, H.T.,Cartailler, J.P.,Lanyi, J.K.
Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution.
Science, 286:255-260, 1999

PubMed Abstract: Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8 and 2.0 angstroms resolution, respectively. The trapped photoproduct corresponds to the late M state in the transport cycle-that is, after proton transfer to Asp85 and release of a proton to the extracellular membrane surface, but before reprotonation of the deprotonated retinal Schiff base. Its density map describes displacements of side chains near the retinal induced by its photoisomerization to 13-cis,15-anti and an extensive rearrangement of the three-dimensional network of hydrogen-bonded residues and bound water that accounts for the changed pKa values (where Ka is the acid constant) of the Schiff base and Asp85. The structural changes detected suggest the means for conserving energy at the active site and for ensuring the directionality of proton translocation.

PubMed: 10514362
DOI: 10.1126/science.286.5438.255

Experimental method

X-RAY DIFFRACTION (2 Å)