2fcp: Difference between revisions
New page: left|200px<br /><applet load="2fcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fcp, resolution 2.50Å" /> '''FERRIC HYDROXAMATE U... |
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[[Image:2fcp.jpg|left|200px]]<br /><applet load="2fcp" size=" | [[Image:2fcp.jpg|left|200px]]<br /><applet load="2fcp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fcp, resolution 2.50Å" /> | caption="2fcp, resolution 2.50Å" /> | ||
'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI'''<br /> | '''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI'''<br /> | ||
==Overview== | ==Overview== | ||
FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member | FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta sheet and four short alpha helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane. | ||
==About this Structure== | ==About this Structure== | ||
2FCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, NI, LIL, AAE, LIM and EA2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2FCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=LIL:'>LIL</scene>, <scene name='pdbligand=AAE:'>AAE</scene>, <scene name='pdbligand=LIM:'>LIM</scene> and <scene name='pdbligand=EA2:'>EA2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
[[Category: Ferguson, A | [[Category: Ferguson, A D.]] | ||
[[Category: Hofmann, E.]] | [[Category: Hofmann, E.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
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[[Category: tonb-dependent receptor]] | [[Category: tonb-dependent receptor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:00 2008'' | ||
Revision as of 18:20, 21 February 2008
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FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI
OverviewOverview
FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta sheet and four short alpha helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.
About this StructureAbout this Structure
2FCP is a Single protein structure of sequence from Escherichia coli with , , , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide., Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W, Science. 1998 Dec 18;282(5397):2215-20. PMID:9856937
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