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4OV0

Structure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase

Summary for 4OV0
Entry DOI10.2210/pdb4ov0/pdb
DescriptorBacteriorhodopsin, RETINAL (3 entities in total)
Functional Keywordslight-driven proton pump, retinal attached via schiff base, membrane, transport protein
Biological sourceHalobacterium sp.
Cellular locationCell membrane ; Multi-pass membrane protein : P02945
Total number of polymer chains1
Total formula weight27213.94
Authors
Primary citationPolovinkin, V.,Gushchin, I.,Sintsov, M.,Round, E.,Balandin, T.,Chervakov, P.,Schevchenko, V.,Utrobin, P.,Popov, A.,Borshchevskiy, V.,Mishin, A.,Kuklin, A.,Willbold, D.,Chupin, V.,Popot, J.L.,Gordeliy, V.
High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase.
J.Membr.Biol., 247:997-1004, 2014
Cited by
PubMed Abstract: Amphipols (APols) have become important tools for the stabilization, folding, and in vitro structural and functional studies of membrane proteins (MPs). Direct crystallization of MPs solubilized in APols would be of high importance for structural biology. However, despite considerable efforts, it is still not clear whether MP/APol complexes can form well-ordered crystals suitable for X-ray crystallography. In the present work, we show that an APol-trapped MP can be crystallized in meso. Bacteriorhodopsin (BR) trapped by APol A8-35 was mixed with a lipidic mesophase, and crystallization was induced by adding a precipitant. The crystals diffract beyond 2 Å. The structure of BR was solved to 2 Å and found to be indistinguishable from previous structures obtained after transfer from detergent solutions. We suggest the proposed protocol of in meso crystallization to be generally applicable to APol-trapped MPs.
PubMed: 25192977
DOI: 10.1007/s00232-014-9700-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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