2d1g | pdb_00002d1g

Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate

spinqualitylabelsall models 2d1g, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2d1g is a 2 chain structure with sequence from Francisella novicida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DVT, ETE, ETX, PGE, UNX, VO4 Gene: acpA (Francisella novicida) Activity: Acid phosphatase, with EC number 3.1.3.2 Resources: FirstGlance, OCA, RCSB, PDBsum 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 AcpA is a respiratory burst-inhibiting acid phosphatase from the Centers for Disease Control and Prevention Category A bioterrorism agent Francisella tularensis and prototype of a superfamily of acid phosphatases and phospholipases C. We report the 1.75-A resolution crystal structure of AcpA complexed with the inhibitor orthovanadate, which is the first structure of any F. tularensis protein and the first for any member of this superfamily. The core domain is a twisted 8-stranded beta-sheet flanked by three alpha-helices on either side, with the active site located above the carboxyl-terminal edge of the beta-sheet. This architecture is unique among acid phosphatases and resembles that of alkaline phosphatase. Unexpectedly, the active site features a serine nucleophile and metal ion with octahedral coordination. Structure-based sequence analysis of the AcpA superfamily predicts that the hydroxyl nucleophile and metal center are also present in AcpA-like phospholipases C. These results imply a phospholipase C catalytic mechanism that is radically different from that of zinc metallophospholipases. Structure of Francisella tularensis AcpA: prototype of a unique superfamily of acid phosphatases and phospholipases C.,Felts RL, Reilly TJ, Tanner JJ J Biol Chem. 2006 Oct 6;281(40):30289-98. Epub 2006 Aug 9. PMID:16899453 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase

Proteopedia Page Contributors and Editors (what is this?)

OCA