1g90: Difference between revisions
New page: left|200px<br /><applet load="1g90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g90" /> '''NMR Solution Structure of Outer Membrane Pro... |
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[[Image:1g90.gif|left|200px]]<br /><applet load="1g90" size=" | [[Image:1g90.gif|left|200px]]<br /><applet load="1g90" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers'''<br /> | '''NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers'''<br /> | ||
==Overview== | ==Overview== | ||
We have determined the three-dimensional fold of the 19 kDa (177 residues) | 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== | ==About this Structure== | ||
1G90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1G90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G90 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Abildgaard, F.]] | [[Category: Abildgaard, F.]] | ||
[[Category: Arora, A.]] | [[Category: Arora, A.]] | ||
[[Category: Bushweller, J | [[Category: Bushweller, J H.]] | ||
[[Category: Tamm, L | [[Category: Tamm, L K.]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
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Revision as of 13:47, 21 February 2008
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NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers
OverviewOverview
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 StructureAbout this Structure
1G90 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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