1si0: Difference between revisions
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|PDB= 1si0 |SIZE=350|CAPTION= <scene name='initialview01'>1si0</scene>, resolution 1.35Å | |PDB= 1si0 |SIZE=350|CAPTION= <scene name='initialview01'>1si0</scene>, resolution 1.35Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= fbpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=75985 Mannheimia haemolytica]) | |GENE= fbpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=75985 Mannheimia haemolytica]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1q35|1Q35]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1si0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1si0 OCA], [http://www.ebi.ac.uk/pdbsum/1si0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1si0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Snell, G.]] | [[Category: Snell, G.]] | ||
[[Category: Tari, L W.]] | [[Category: Tari, L W.]] | ||
[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:42:18 2008'' | ||
Revision as of 23:42, 30 March 2008
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| , resolution 1.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | fbpA (Mannheimia haemolytica) | ||||||
| Related: | 1Q35
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in a closed conformation
OverviewOverview
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.
About this StructureAbout this Structure
1SI0 is a Single protein structure of sequence from Mannheimia haemolytica. Full crystallographic information is available from OCA.
ReferenceReference
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
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