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1BM1

CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE

Summary for 1BM1
Entry DOI10.2210/pdb1bm1/pdb
DescriptorBACTERIORHODOPSIN, 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 Keywordsproton pump, membrane protein, retinal protein, photoreceptor
Biological sourceHalobacterium salinarum
Cellular locationCell membrane; Multi-pass membrane protein: P02945
Total number of polymer chains1
Total formula weight27969.01
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 citationSato, 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: 10393291
DOI: 10.1107/S090744499900503X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

226707

数据于2024-10-30公开中

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