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3MOZ

Structure of the PTP-like phytase from Selenomonas ruminantium in complex with myo-inositol (1,2,3,5,6)pentakisphosphate

Summary for 3MOZ
Entry DOI10.2210/pdb3moz/pdb
Related2B4U 3MMJ
DescriptorMyo-inositol hexaphosphate phosphohydrolase, PHOSPHATE ION, (1R,2R,3R,4R,5S,6S)-6-HYDROXYCYCLOHEXANE-1,2,3,4,5-PENTAYL PENTAKIS[DIHYDROGEN (PHOSPHATE)], ... (7 entities in total)
Functional Keywordsphytase, protein tyrosine phosphatase, inositol phosphatase, inositol phosphate, hydrolase
Biological sourceSelenomonas ruminantium
Total number of polymer chains2
Total formula weight74705.36
Authors
Gruninger, R.J.,Selinger, L.B.,Mosimann, S.C. (deposition date: 2010-04-23, release date: 2011-06-22, Last modification date: 2023-09-06)
Primary citationGruninger, R.J.,Dobing, S.,Smith, A.D.,Bruder, L.M.,Selinger, L.B.,Wieden, H.J.,Mosimann, S.C.
Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.
J.Biol.Chem., 287:9722-9730, 2012
Cited by
PubMed Abstract: Protein-tyrosine phosphatase-like inositol polyphosphatases are microbial enzymes that catalyze the stepwise removal of one or more phosphates from highly phosphorylated myo-inositols via a relatively ordered pathway. To understand the substrate specificity and kinetic mechanism of these enzymes we have determined high resolution, single crystal, x-ray crystallographic structures of inactive Selenomonas ruminantium PhyA in complex with myo-inositol hexa- and pentakisphosphate. These structures provide the first glimpse of a myo-inositol polyphosphatase-ligand complex consistent with its known specificity and reveal novel features of the kinetic mechanism. To complement the structural studies, fluorescent binding assays have been developed and demonstrate that the K(d) for this enzyme is several orders of magnitude lower than the K(m). Together with rapid kinetics data, these results suggest that the protein tyrosine phosphatase-like inositol polyphosphatases have a two-step, substrate-binding mechanism that facilitates catalysis.
PubMed: 22139834
DOI: 10.1074/jbc.M111.309872
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

239803

数据于2025-08-06公开中

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