3c7t

Crystal structure of the ecdysone phosphate phosphatase, EPPase, from Bombix mori in complex with tungstate

spinqualitylabelsall models 3c7t, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3c7t is a 4 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.76Å Ligands: CL, IOD, MG, NA, WO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EPP_BOMMO Steroid phosphatase which catalyzes the conversion of inactive phosphorylated ecdysteroids into their active forms (PubMed:12721294, PubMed:15738639, PubMed:18937503). Shows high activity towards ecdysone 22-phosphate (E22P) (PubMed:12721294). Has lower activity towards other ecdysteriod phosphates including 20-hydroxyecdysone 22-phosphate (20E22P) and 2-deoxyecdysone 22-phosphate (2dE22P) (PubMed:12721294). Also has protein tyrosine phosphatase activity (PubMed:18937503). 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 Here, we present the crystal structure of the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a steroid phosphate phosphatase. The structure reveals an alpha/beta-fold common to members of the two histidine (2H)-phosphatase superfamily with strong homology to the Suppressor of T-cell receptor signaling-1 (Sts-1 PGM) protein. The putative EPPase PGM active site contains signature residues shared by 2H-phosphatase enzymes, including a conserved histidine (His80) that acts as a nucleophile during catalysis. The physiological substrate ecdysone 22-phosphate was modeled in a hydrophobic cavity close to the phosphate-binding site. EPPase PGM shows limited substrate specificity with an ability to hydrolyze steroid phosphates, the phospho-tyrosine (pTyr) substrate analogue para-nitrophenylphosphate ( pNPP) and pTyr-containing peptides and proteins. Altogether, our data demonstrate a new protein tyrosine phosphatase (PTP) activity for EPPase. They suggest that EPPase and its closest homologues can be grouped into a distinct subfamily in the large 2H-phosphatase superfamily of proteins. Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from bombyx mori reveals a new enzymatic activity.,Chen Y, Jakoncic J, Wang J, Zheng X, Carpino N, Nassar N Biochemistry. 2008 Nov 18;47(46):12135-45. Epub 2008 Oct 21. PMID:18937503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA