1si1: Difference between revisions
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<StructureSection load='1si1' size='340' side='right'caption='[[1si1]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='1si1' size='340' side='right'caption='[[1si1]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1si1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1si1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SI1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=1si1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si1 OCA], [https://pdbe.org/1si1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1si1 RCSB], [https://www.ebi.ac.uk/pdbsum/1si1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1si1 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9Z4N6_MANHA Q9Z4N6_MANHA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1si1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1si1" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ferric-binding protein|Ferric-binding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dougan | [[Category: Mannheimia haemolytica]] | ||
[[Category: McRee | [[Category: Dougan DR]] | ||
[[Category: Schryvers | [[Category: McRee DE]] | ||
[[Category: Shouldice | [[Category: Schryvers AB]] | ||
[[Category: Skene | [[Category: Shouldice SR]] | ||
[[Category: Snell | [[Category: Skene RJ]] | ||
[[Category: Tari | [[Category: Snell G]] | ||
[[Category: Tari LW]] | |||
Latest revision as of 09:17, 23 August 2023
Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformationCrystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open conformation
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the 1.35- and 1.45-A structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe(3+)) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm. Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens.,Shouldice SR, Skene RJ, Dougan DR, Snell G, McRee DE, Schryvers AB, Tari LW J Bacteriol. 2004 Jun;186(12):3903-10. PMID:15175304[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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