1q35
From Proteopedia
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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 EDO and FMT 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
Page seeded by OCA on Sun Nov 25 03:29:34 2007
