2ei4: Difference between revisions

Revision as of 08:39, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ei4.png

Template:STRUCTURE 2ei4

Trimeric complex of archaerhodopsin-2Trimeric complex of archaerhodopsin-2

Template:ABSTRACT PUBMED 18082767

About this StructureAbout this Structure

2EI4 is a Single protein structure of sequence from Halobacterium sp.. Full crystallographic information is available from OCA.

ReferenceReference

Structural role of bacterioruberin in the trimeric structure of archaerhodopsin-2., Yoshimura K, Kouyama T, J Mol Biol. 2008 Feb 1;375(5):1267-81. Epub 2007 Nov 22. PMID:18082767

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OCA

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-[[Image:2ei4.jpg|left|200px]]
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 {{STRUCTURE_2ei4|  PDB=2ei4  |  SCENE=  }}
-'''Trimeric complex of archaerhodopsin-2'''
+===Trimeric complex of archaerhodopsin-2===
-==Overview==
+<!--
-Archaerhodopsin-2 (aR2), a retinal protein-carotenoid complex found in the claret membrane of Halorubrum sp. aus-2, functions as a light-driven proton pump. In this study, the membrane fusion method was utilized to prepare trigonal P321 crystals (a=b=98.2 A, c=56.2 A) and hexagonal P6(3) crystals (a=b=108.8 A, c=220.7 A). The trigonal crystal is made up of stacked membranes in which the aR2 trimers are arranged on a honeycomb lattice. Similar membranous structures are found in the hexagonal crystal, but four membrane layers with different orientations are contained in the unit cell. In these crystals, the carotenoid bacterioruberin [5,32-bis(2-hydroxypropan-2-yl)-2,8,12,16,21,25,29,35-octamethylhexatriaco nta-6,8,10,12,14,16,18,20,22,24,26,28,30-tridecaene-2,35-diol] binds to crevices between the subunits of the trimer. Its polyene chain is inclined from the membrane normal by an angle of about 20 degrees and, on the cytoplasmic side, it is surrounded by helices AB and DE of neighbouring subunits. This peculiar binding mode suggests that bacterioruberin plays a striking structural role for the trimerization of aR2. When compared with the aR2 structure in another crystal form containing no bacterioruberin, the proton release channel takes a more closed conformation in the P321 or P6(3) crystal; i.e., the native conformation of protein is stabilized in the trimeric protein-bacterioruberin complex. Interestingly, most residues participating in the trimerization are not conserved in bacteriorhodopsin, a homologous protein capable of forming a trimeric structure in the absence of bacterioruberin. Despite a large alteration in the amino acid sequence, the shape of the intratrimer hydrophobic space filled by lipids is highly conserved between aR2 and bacteriorhodopsin. Since a transmembrane helix facing this space undergoes a large conformational change during the proton pumping cycle, it is feasible that trimerization is an important strategy to capture special lipid components that are relevant to the protein activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_18082767}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18082767 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18082767}}
 ==About this Structure==
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 [[Category: Retinal]]
 [[Category: Transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:35:10 2008''
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