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| | <StructureSection load='3nrq' size='340' side='right'caption='[[3nrq]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3nrq' size='340' side='right'caption='[[3nrq]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nrq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_f11 Escherichia coli f11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NRQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nrq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_F11 Escherichia coli F11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NRQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nrp|3nrp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EcF11_1994 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340197 Escherichia coli F11])</td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrq OCA], [https://pdbe.org/3nrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nrq RCSB], [https://www.ebi.ac.uk/pdbsum/3nrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nrq ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nrq OCA], [https://pdbe.org/3nrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nrq RCSB], [https://www.ebi.ac.uk/pdbsum/3nrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nrq ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli f11]] | + | [[Category: Escherichia coli F11]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chan, A C.K]] | + | [[Category: Chan ACK]] |
| - | [[Category: Murphy, M E.P]] | + | [[Category: Murphy MEP]] |
| - | [[Category: Copper binding]]
| + | |
| - | [[Category: Immunoglobulin-like fold]]
| + | |
| - | [[Category: Iron transporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
In the uropathogenic Escherichia coli strain F11, in silico genome analysis revealed the dicistronic iron uptake operon fetMP, which is under iron-regulated control mediated by the Fur regulator. The expression of fetMP in a mutant strain lacking known iron uptake systems improved growth under iron depletion and increased cellular iron accumulation. FetM is a member of the iron/lead transporter superfamily and is essential for iron uptake by the Fet system. FetP is a periplasmic protein that enhanced iron uptake by FetM. Recombinant FetP bound Cu(II) and the iron analog Mn(II) at distinct sites. The crystal structure of the FetP dimer reveals a copper site in each FetP subunit that adopts two conformations: CuA with a tetrahedral geometry composed of His(44), Met(90), His(97), and His(127), and CuB, a second degenerate octahedral geometry with the addition of Glu(46). The copper ions of each site occupy distinct positions and are separated by approximately 1.3 A. Nearby, a putative additional Cu(I) binding site is proposed as an electron source that may function with CuA/CuB displacement to reduce Fe(III) for transport by FetM. Together, these data indicate that FetMP is an additional iron uptake system composed of a putative iron permease and an iron-scavenging and potentially iron-reducing periplasmic protein.
Characterization of a Dipartite Iron Uptake System from Uropathogenic Escherichia coli Strain F11.,Koch D, Chan AC, Murphy ME, Lilie H, Grass G, Nies DH J Biol Chem. 2011 Jul 15;286(28):25317-30. Epub 2011 May 19. PMID:21596746[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koch D, Chan AC, Murphy ME, Lilie H, Grass G, Nies DH. Characterization of a Dipartite Iron Uptake System from Uropathogenic Escherichia coli Strain F11. J Biol Chem. 2011 Jul 15;286(28):25317-30. Epub 2011 May 19. PMID:21596746 doi:10.1074/jbc.M111.222745
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