1q35
From Proteopedia
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|PDB= 1q35 |SIZE=350|CAPTION= <scene name='initialview01'>1q35</scene>, resolution 1.20Å | |PDB= 1q35 |SIZE=350|CAPTION= <scene name='initialview01'>1q35</scene>, resolution 1.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q35 OCA], [http://www.ebi.ac.uk/pdbsum/1q35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q35 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tari, L W.]] | [[Category: Tari, L W.]] | ||
[[Category: Williams, P A.]] | [[Category: Williams, P A.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: FMT]] | ||
[[Category: iron binding protein]] | [[Category: iron 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 23:08:12 2008'' |
Revision as of 20:08, 30 March 2008
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| , resolution 1.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | fbpA (Mannheimia haemolytica) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A
Overview
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.
About this Structure
1Q35 is a Single protein structure of sequence from Mannheimia haemolytica. Full crystallographic information is available from OCA.
Reference
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
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