1j9l

CRYSTAL STRUCTURE OF SURE PROTEIN FROM T.MARITIMA IN COMPLEX WITH VANADATE

spinqualitylabelsall models 1j9l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1j9l is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CA, EPE, VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SURE_THEMA Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.[HAMAP-Rule:MF_00060] 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 Homologs of the Escherichia coli surE gene are present in many eubacteria and archaea. Despite the evolutionary conservation, little information is available on the structure and function of their gene products. We have determined the crystal structure of the SurE protein from Thermotoga maritima. The structure reveals the dimeric arrangement of the subunits and an active site around a bound metal ion. We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate. In the vanadate- and tungstate-complexed structures, the inhibitors bind adjacent to the divalent metal ion. Our structural and functional analyses identify the SurE proteins as a novel family of metal ion-dependent phosphatases. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.,Lee JY, Kwak JE, Moon J, Eom SH, Liong EC, Pedelacq JD, Berendzen J, Suh SW Nat Struct Biol. 2001 Sep;8(9):789-94. PMID:11524683 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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