3nrq
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3nrq is ON HOLD Authors: Chan, A.C.K., Murphy, M.E.P. Description: Crystal structure of copper-reconstituted FetP from uropathogenic Escherichia co...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of copper-reconstituted FetP from uropathogenic Escherichia coli strain F11== | |
| + | <StructureSection load='3nrq' size='340' side='right'caption='[[3nrq]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == 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> | ||
| + | </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='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='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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21596746</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3nrq" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli F11]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chan ACK]] | ||
| + | [[Category: Murphy MEP]] | ||
Current revision
Crystal structure of copper-reconstituted FetP from uropathogenic Escherichia coli strain F11
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