1Q35
Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A
Summary for 1Q35
| Entry DOI | 10.2210/pdb1q35/pdb |
| Descriptor | iron binding protein FbpA, 1,2-ETHANEDIOL, FORMIC ACID, ... (4 entities in total) |
| Functional Keywords | iron binding protein, metal binding protein |
| Biological source | Mannheimia haemolytica |
| Total number of polymer chains | 1 |
| Total formula weight | 36048.92 |
| Authors | Shouldice, S.R.,Dougan, D.R.,Skene, R.J.,Snell, G.,Scheibe, D.,Williams, P.A.,Kirby, S.,McRee, D.E.,Schryvers, A.B.,Tari, L.W. (deposition date: 2003-07-28, release date: 2003-11-11, Last modification date: 2024-11-13) |
| Primary citation | Shouldice, S.R.,Dougan, D.R.,Williams, P.A.,Skene, R.J.,Snell, G.,Scheibe, D.,Kirby, S.,Hosfield, D.J.,McRee, D.E.,Schryvers, A.B.,Tari, L.W. Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins J.Biol.Chem., 278:41093-41098, 2003 Cited by PubMed Abstract: 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. PubMed: 12882966DOI: 10.1074/jbc.M306821200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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