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| [[Image:1q35.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1q35| PDB=1q35 | SCENE= }} | | {{STRUCTURE_1q35| PDB=1q35 | SCENE= }} |
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| '''Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A'''
| | ===Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12882966}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12882966 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12882966}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Williams, P A.]] | | [[Category: Williams, P A.]] |
| [[Category: Iron binding protein]] | | [[Category: Iron binding protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:48:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:17:18 2008'' |
