1kmo
From Proteopedia
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|PDB= 1kmo |SIZE=350|CAPTION= <scene name='initialview01'>1kmo</scene>, resolution 2.00Å | |PDB= 1kmo |SIZE=350|CAPTION= <scene name='initialview01'>1kmo</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= fecA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= fecA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kmp|1kmp]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmo OCA], [http://www.ebi.ac.uk/pdbsum/1kmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kmo RCSB]</span> | ||
}} | }} | ||
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[[Category: Helm, D van der.]] | [[Category: Helm, D van der.]] | ||
[[Category: Smith, B S.]] | [[Category: Smith, B S.]] | ||
| - | [[Category: HTO]] | ||
| - | [[Category: LDA]] | ||
[[Category: iron transporter]] | [[Category: iron transporter]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: tonb-dependent receptor]] | [[Category: tonb-dependent receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:50:40 2008'' |
Revision as of 18:50, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | fecA (Escherichia coli) | ||||||
| Related: | 1kmp
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Outer Membrane Transporter FecA
Overview
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.
About this Structure
1KMO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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