1brx: Difference between revisions

Revision as of 19:37, 30 June 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:1brx.png

Template:STRUCTURE 1brx

BACTERIORHODOPSIN/LIPID COMPLEXBACTERIORHODOPSIN/LIPID COMPLEX

Template:ABSTRACT PUBMED 9632391

About this StructureAbout this Structure

1BRX is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

ReferenceReference

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution., Luecke H, Richter HT, Lanyi JK, Science. 1998 Jun 19;280(5371):1934-7. PMID:9632391

Page seeded by OCA on Mon Jun 30 19:37:43 2008

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OCA

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-[[Image:1brx.gif|left|200px]]
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 {{STRUCTURE_1brx|  PDB=1brx  |  SCENE=  }}
-'''BACTERIORHODOPSIN/LIPID COMPLEX'''
+===BACTERIORHODOPSIN/LIPID COMPLEX===
-==Overview==
+<!--
-Photoisomerization of the retinal of bacteriorhodopsin initiates a cyclic reaction in which a proton is translocated across the membrane. Studies of this protein promise a better understanding of how ion pumps function. Together with a large amount of spectroscopic and mutational data, the atomic structure of bacteriorhodopsin, determined in the last decade at increasing resolutions, has suggested plausible but often contradictory mechanisms. X-ray diffraction of bacteriorhodopsin crystals grown in cubic lipid phase revealed unexpected two-fold symmetries that indicate merohedral twinning along the crystallographic c axis. The structure, refined to 2.3 angstroms taking this twinning into account, is different from earlier models, including that most recently reported. One of the carboxyl oxygen atoms of the proton acceptor Asp85 is connected to the proton donor, the retinal Schiff base, through a hydrogen-bonded water and forms a second hydrogen bond with another water. The other carboxyl oxygen atom of Asp85 accepts a hydrogen bond from Thr89. This structure forms the active site. The nearby Arg82 is the center of a network of numerous hydrogen-bonded residues and an ordered water molecule. This network defines the pathway of the proton from the buried Schiff base to the extracellular surface.
+The line below this paragraph, {{ABSTRACT_PUBMED_9632391}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9632391 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9632391}}
 ==About this Structure==
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 [[Category: Proton pump]]
 [[Category: Retinal protein]]
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