1kme

(Difference between revisions)

Categories: Halobacterium salinarum | Single protein | Bowie, J U. | Faham, S. | Membrane protein

Revision as of 07:33, 2 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.

Image:1kme.png

1kme, resolution 2.00Å ()

Ligands:

, ,

Structural annotation:
Resources:	CATH : 1Kmea00, 1Kmeb00 InterPro : Ipr001425 Pfam : PF01036 SCOP : d1kmea_, d1kmeb_ UniProt : P02945

Functional annotation:
Cellular component:	membrane integral to membrane
Biological process:	response to stimulus transport protein-chromophore linkage phototransduction ion transport proton transport
Molecular function:	hydrogen ion transmembrane transporter activity photoreceptor activity receptor activity ion channel activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES

Template:ABSTRACT PUBMED 11829498

About this Structure

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

Reference

Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure., Faham S, Bowie JU, J Mol Biol. 2002 Feb 8;316(1):1-6. PMID:11829498

Page seeded by OCA on Wed Jul 2 10:33:12 2008

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kme"

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-'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES'''
+===CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES===
-==Overview==
+<!--
-Obtaining crystals of membrane proteins that diffract to high resolution remains a major stumbling block in structure determination. Here we present a new method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture. The method is flexible and simple to use. As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was crystallized from a bicellar solution, yielding a new bR crystal form. The crystals belong to space group P2(1) with unit cell dimensions of a=45.0 A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit. The structure was solved by molecular replacement and refined at 2.0 A resolution. In all previous bR structures the protein is organized as a parallel trimer, but in the crystals grown from bicelles, the individual bR subunits are arranged in an antiparallel fashion.
+The line below this paragraph, {{ABSTRACT_PUBMED_11829498}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11829498 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11829498}}
 ==About this Structure==
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