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| | <StructureSection load='1si0' size='340' side='right'caption='[[1si0]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='1si0' size='340' side='right'caption='[[1si0]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1si0]] 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=1SI0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SI0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1si0]] 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=1SI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SI0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q35|1q35]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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'>[https://proteopedia.org/fgij/fg.htm?mol=1si0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si0 OCA], [https://pdbe.org/1si0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1si0 RCSB], [https://www.ebi.ac.uk/pdbsum/1si0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1si0 ProSAT]</span></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=1si0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si0 OCA], [http://pdbe.org/1si0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1si0 RCSB], [http://www.ebi.ac.uk/pdbsum/1si0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1si0 ProSAT]</span></td></tr> | + | |
| | </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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33396]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dougan, D R]] | + | [[Category: Mannheimia haemolytica]] |
| - | [[Category: McRee, D E]] | + | [[Category: Dougan DR]] |
| - | [[Category: Schryvers, A B]] | + | [[Category: McRee DE]] |
| - | [[Category: Shouldice, S R]] | + | [[Category: Schryvers AB]] |
| - | [[Category: Skene, R J]] | + | [[Category: Shouldice SR]] |
| - | [[Category: Snell, G]] | + | [[Category: Skene RJ]] |
| - | [[Category: Tari, L W]] | + | [[Category: Snell G]] |
| - | [[Category: Metal binding protein]]
| + | [[Category: Tari LW]] |
| Structural highlights
Function
Q9Z4N6_MANHA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We 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.
References
- ↑ Shouldice SR, Skene RJ, Dougan DR, Snell G, McRee DE, Schryvers AB, Tari LW. Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens. J Bacteriol. 2004 Jun;186(12):3903-10. PMID:15175304 doi:10.1128/JB.186.12.3903-3910.2004
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