1brr
From Proteopedia
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X-RAY STRUCTURE OF THE BACTERIORHODOPSIN TRIMER/LIPID COMPLEX
Overview
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.
About this Structure
1BRR is a Single protein structure of sequence from Halobacterium salinarum with GLC, RET, ARC, OCT and GOL as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 11:51:55 2007
Categories: Halobacterium salinarum | Single protein | Essen, L.O. | Oesterhelt, D. | Siegert, R. | ARC | GLC | GOL | OCT | RET | Haloarchaea | Lipids | Membrane protein | Photoreceptor | Proton pump | Retinal protein
