2d1g

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spinqualitylabelsall models 2d1g, resolution 1.750Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2D1G is a Single protein structure of sequence from Francisella tularensis subsp. novicida with , , , , and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.

Reference

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

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