1q35

<table><tr><td colspan='2'>[[1q35]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33396 Atcc 33396]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q35 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q35 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fbpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=75985 ATCC 33396])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q35 OCA], [http://pdbe.org/1q35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q35 RCSB], [http://www.ebi.ac.uk/pdbsum/1q35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q35 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Pasteurellosis caused by the Gram-negative pathogen Pasteurella haemolytica is a serious disease leading to death in cattle. To scavenge growth-limiting iron from the host, the pathogen utilizes the periplasmic ferric ion-binding protein A (PhFbpA) as a component of an ATP-binding cassette transport pathway. We report the 1.2-A structure of the iron-free (apo) form of PhFbpA, which is a member of the transferrin structural superfamily. The protein structure adopts a closed conformation, allowing us to reliably assign putative iron-coordinating residues. Based on our analysis, PhFbpA utilizes a unique constellation of binding site residues and anions to octahedrally coordinate an iron atom. A surprising finding in the structure is the presence of two formate anions on opposite sides of the iron-binding pocket. The formate ions tether the N- and C-terminal domains of the protein and stabilize the closed structure, also providing clues as to probable candidates for synergistic anions in the iron-loaded state. PhFbpA represents a new class of bacterial iron-binding proteins.

Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins.,Shouldice SR, Dougan DR, Williams PA, Skene RJ, Snell G, Scheibe D, Kirby S, Hosfield DJ, McRee DE, Schryvers AB, Tari LW J Biol Chem. 2003 Oct 17;278(42):41093-8. Epub 2003 Jul 25. PMID:12882966<ref>PMID:12882966</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 33396]]

[[Category: Dougan, D R]]

[[Category: Kirby, S]]

[[Category: McRee, D E]]

[[Category: Scheibe, D]]

[[Category: Schryvers, A B]]

[[Category: Shouldice, S R]]

[[Category: Skene, R J]]

[[Category: Snell, G]]

[[Category: Tari, L W]]

[[Category: Williams, P A]]

[[Category: Metal binding protein]]