4amf | pdb_00004amf

Pseudomonas fluorescens PhoX in complex with the substrate analogue AppCp

spinqualitylabelsall models 4amf, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4amf is a 2 chain structure with sequence from Pseudomonas fluorescens Pf0-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: ACP, CA, CL, EDO, FEO, LI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3K5N8_PSEPF Publication Abstract from PubMed Alkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes, we have determined the structure of the widely occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active-site cofactor comprising two antiferromagnetically coupled ferric iron ions (Fe(3+)), three calcium ions (Ca(2+)), and an oxo group bridging three of the metal ions. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active-site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition. A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.,Yong SC, Roversi P, Lillington J, Rodriguez F, Krehenbrink M, Zeldin OB, Garman EF, Lea SM, Berks BC Science. 2014 Sep 5;345(6201):1170-3. doi: 10.1126/science.1254237. PMID:25190793 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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