1q35
From Proteopedia
(New page: 200px<br /><applet load="1q35" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q35, resolution 1.20Å" /> '''Crystal Structure of...) |
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| - | [[Image:1q35.gif|left|200px]]<br /><applet load="1q35" size=" | + | [[Image:1q35.gif|left|200px]]<br /><applet load="1q35" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q35, resolution 1.20Å" /> | caption="1q35, resolution 1.20Å" /> | ||
'''Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A'''<br /> | '''Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pasteurellosis caused by the Gram-negative pathogen Pasteurella | + | 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== | ==About this Structure== | ||
| - | 1Q35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica] with EDO and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Q35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica] with <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q35 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mannheimia haemolytica]] | [[Category: Mannheimia haemolytica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dougan, D | + | [[Category: Dougan, D R.]] |
[[Category: Kirby, S.]] | [[Category: Kirby, S.]] | ||
| - | [[Category: McRee, D | + | [[Category: McRee, D E.]] |
[[Category: Scheibe, D.]] | [[Category: Scheibe, D.]] | ||
| - | [[Category: Schryvers, A | + | [[Category: Schryvers, A B.]] |
| - | [[Category: Shouldice, S | + | [[Category: Shouldice, S R.]] |
| - | [[Category: Skene, R | + | [[Category: Skene, R J.]] |
[[Category: Snell, G.]] | [[Category: Snell, G.]] | ||
| - | [[Category: Tari, L | + | [[Category: Tari, L W.]] |
| - | [[Category: Williams, P | + | [[Category: Williams, P A.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: iron binding protein]] | [[Category: iron binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:20 2008'' |
Revision as of 12:35, 21 February 2008
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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 with and as ligands. 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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