2ozx

Solution structure of human phosphohistidine phosphatase 1 in phosphate free form

spinqualitylabelsall models 2ozx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ozx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHP14_HUMAN Exhibits phosphohistidine phosphatase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Protein histidine phosphorylation exists widely in vertebrates, and it plays important roles in signal transduction and other cellular functions. However, knowledge about eukaryotic PHPT (protein histidine phosphatase) is still very limited. To date, only one vertebrate PHPT has been discovered, and two crystal structures of hPHPT1 (human PHPT1) have been solved. However, these two structures gave different ligand-binding sites and co-ordination patterns. In the present paper, we have solved the solution structures of hPHPT1 in both P(i)-free and P(i)-bound states. Through comparison of the structures, along with a mutagenesis study, we have determined the active site of hPHPT1. In contrast with previous results, our results indicate that the active site is located between helix alpha1 and loop L5. His(53) was identified to be the catalytic residue, and the NH groups of residues His(53), Ala(54) and Ala(96) and the OH group of Ser(94) should act as anchors of P(i) or substrate by forming H-bonds with P(i). On the basis of our results, a catalytic mechanism is proposed for hPHPT1: the imidazole ring of His(53) serves as a general base to activate a water molecule, and the activated water would attack the substrate as a nucleophile in the catalysis; the positively charged side chain of Lys(21) can help stabilize the transition state. No similar catalytic mechanism can be found in the EzCatDB database. Solution structure and catalytic mechanism of human protein histidine phosphatase 1.,Gong W, Li Y, Cui G, Hu J, Fang H, Jin C, Xia B Biochem J. 2009 Mar 1;418(2):337-44. PMID:18991813 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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