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1brr
From Proteopedia
Revision as of 09:49, 13 August 2014 by OCA (Talk | contribs)
1brr is a 3 chain structure with sequence from Halobacterium salinarum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Heterogenous nucleation on small molecule crystals causes a monoclinic crystal form of bacteriorhodopsin (BR) in which trimers of this membrane protein pack differently than in native purple membranes. Analysis of single crystals by nano-electrospray ionization-mass spectrometry demonstrated a preservation of the purple membrane lipid composition in these BR crystals. The 2.9-A x-ray structure shows a lipid-mediated stabilization of BR trimers where the glycolipid S-TGA-1 binds into the central compartment of BR trimers. The BR trimer/lipid complex provides an example of local membrane thinning as the lipid head-group boundary of the central lipid patch is shifted by 5 A toward the membrane center. Nonbiased electron density maps reveal structural differences to previously reported BR structures, especially for the cytosolic EF loop and the proton exit pathway. The terminal proton release complex now comprises an E194-E204 dyad as a diffuse proton buffer.
Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex.,Essen L, Siegert R, Lehmann WD, Oesterhelt D Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11673-8. PMID:9751724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Essen L, Siegert R, Lehmann WD, Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11673-8. PMID:9751724
