1si1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1si1]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SI1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1si1]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SI1 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q35|1q35]], [[1si0|1si0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q35|1q35]], [[1si0|1si0]]</td></tr> | ||
<tr><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 Mannheimia haemolytica])</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 Mannheimia haemolytica])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1si1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1si1 RCSB], [http://www.ebi.ac.uk/pdbsum/1si1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1si1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1si1 RCSB], [http://www.ebi.ac.uk/pdbsum/1si1 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 31: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Mannheimia haemolytica]] | [[Category: Mannheimia haemolytica]] | ||
[[Category: Dougan, D R | [[Category: Dougan, D R]] | ||
[[Category: McRee, D E | [[Category: McRee, D E]] | ||
[[Category: Schryvers, A B | [[Category: Schryvers, A B]] | ||
[[Category: Shouldice, S R | [[Category: Shouldice, S R]] | ||
[[Category: Skene, R J | [[Category: Skene, R J]] | ||
[[Category: Snell, G | [[Category: Snell, G]] | ||
[[Category: Tari, L W | [[Category: Tari, L W]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
Revision as of 10:20, 6 January 2015
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
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 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. References
|
| ||||||||||||||||||||