1BM1
CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE
Summary for 1BM1
Entry DOI | 10.2210/pdb1bm1/pdb |
Descriptor | BACTERIORHODOPSIN, RETINAL, PHOSPHORIC ACID 2,3-BIS-(3,7,11,15-TETRAMETHYL-HEXADECYLOXY)-PROPYL ESTER 2-HYDROXO-3-PHOSPHONOOXY-PROPYL ESTER (3 entities in total) |
Functional Keywords | proton pump, membrane protein, retinal protein, photoreceptor |
Biological source | Halobacterium salinarum |
Cellular location | Cell membrane; Multi-pass membrane protein: P02945 |
Total number of polymer chains | 1 |
Total formula weight | 27969.01 |
Authors | Sato, H.,Takeda, K.,Tani, K.,Hino, T.,Okada, T.,Nakasako, M.,Kamiya, N.,Kouyama, T. (deposition date: 1998-07-28, release date: 1999-04-27, Last modification date: 2023-08-02) |
Primary citation | Sato, H.,Takeda, K.,Tani, K.,Hino, T.,Okada, T.,Nakasako, M.,Kamiya, N.,Kouyama, T. Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin. Acta Crystallogr.,Sect.D, 55:1251-1256, 1999 Cited by PubMed Abstract: In the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer. PubMed: 10393291DOI: 10.1107/S090744499900503X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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