1fcp: Difference between revisions

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[[Image:1fcp.gif|left|200px]]<br /><applet load="1fcp" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fcp.gif|left|200px]]
caption="1fcp, resolution 2.70&Aring;" />
 
'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON'''<br />
{{Structure
|PDB= 1fcp |SIZE=350|CAPTION= <scene name='initialview01'>1fcp</scene>, resolution 2.70&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=LIL:2-TRIDECANOYLOXY-PENTADECANOIC+ACID'>LIL</scene>, <scene name='pdbligand=AAE:ACETOACETIC+ACID'>AAE</scene>, <scene name='pdbligand=LIM:3-OXO-PENTADECANOIC+ACID'>LIM</scene>, <scene name='pdbligand=EA2:AMINOETHANOLPYROPHOSPHATE'>EA2</scene> and <scene name='pdbligand=FCI:FERRICROCIN-IRON'>FCI</scene>
|ACTIVITY=
|GENE=
}}
 
'''FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FCP 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>, <scene name='pdbligand=EA2:'>EA2</scene> and <scene name='pdbligand=FCI:'>FCI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCP OCA].  
1FCP is a [[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=1FCP OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9856937 9856937]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9856937 9856937]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 26: Line 35:
[[Category: active transport]]
[[Category: active transport]]
[[Category: ferrichrome-iron receptor]]
[[Category: ferrichrome-iron receptor]]
[[Category: integral outer membrane protein ]]
[[Category: integral outer membrane protein]]
[[Category: iron transport protein]]
[[Category: iron transport protein]]
[[Category: tonb-dependent receptor]]
[[Category: tonb-dependent receptor]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:07:24 2008''

Revision as of 09:07, 20 March 2008

File:1fcp.gif


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1fcp, resolution 2.70Å
Ligands: PO4, NI, LIL, AAE, LIM, EA2 and FCI
Coordinates: save as pdb, mmCIF, xml



FERRIC HYDROXAMATE UPTAKE RECEPTOR (FHUA) FROM E.COLI IN COMPLEX WITH BOUND FERRICHROME-IRON


Overview

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

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

Reference

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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