1g90

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|ACTIVITY=
|ACTIVITY=
|GENE= OMPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= OMPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1qjp|1QJP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g90 OCA], [http://www.ebi.ac.uk/pdbsum/1g90 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g90 RCSB]</span>
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}}
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[[Category: nmr]]
[[Category: nmr]]
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Revision as of 17:39, 30 March 2008


PDB ID 1g90

Drag the structure with the mouse to rotate
Gene: OMPA (Escherichia coli)
Related: 1QJP


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers


Overview

We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta-barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C(8)E(4)) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein.

About this Structure

1G90 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy., Arora A, Abildgaard F, Bushweller JH, Tamm LK, Nat Struct Biol. 2001 Apr;8(4):334-8. PMID:11276254

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