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1Q35

Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A

Summary for 1Q35
Entry DOI10.2210/pdb1q35/pdb
Descriptoriron binding protein FbpA, 1,2-ETHANEDIOL, FORMIC ACID, ... (4 entities in total)
Functional Keywordsiron binding protein, metal binding protein
Biological sourceMannheimia haemolytica
Total number of polymer chains1
Total formula weight36048.92
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 citationShouldice, 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: 12882966
DOI: 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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