1d2t

CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE

spinqualitylabelsall models 1d2t, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1d2t is a 1 chain structure with sequence from Shimwellia blattae. 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: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9S1A6_SHIBL 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 The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189. X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.,Ishikawa K, Mihara Y, Gondoh K, Suzuki E, Asano Y EMBO J. 2000 Jun 1;19(11):2412-23. PMID:10835340 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA