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1kmp

From Proteopedia

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Revision as of 07:38, 12 October 2017

Crystal structure of the Outer Membrane Transporter FecA Complexed with Ferric Citrate

Structural highlights

1kmp is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	1kmo
Gene:	fecA (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FECA_ECOLI] FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.

Structural basis of gating by the outer membrane transporter FecA.,Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, Deisenhofer J Science. 2002 Mar 1;295(5560):1715-9. PMID:11872840^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, Deisenhofer J. Structural basis of gating by the outer membrane transporter FecA. Science. 2002 Mar 1;295(5560):1715-9. PMID:11872840 doi:10.1126/science.1067313

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Outer Membrane Transporter FecA Complexed with Ferric Citrate==
 <StructureSection load='1kmp' size='340' side='right' caption='[[1kmp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kmo|1kmo]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fecA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmp OCA], [http://pdbe.org/1kmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmp RCSB], [http://www.ebi.ac.uk/pdbsum/1kmp PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmp OCA], [http://pdbe.org/1kmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmp RCSB], [http://www.ebi.ac.uk/pdbsum/1kmp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmp ProSAT]</span></td></tr>
 </table>
 == Function ==

1kmp

From Proteopedia

Revision as of 07:38, 12 October 2017

Crystal structure of the Outer Membrane Transporter FecA Complexed with Ferric Citrate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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