2zp4 | pdb_00002zp4

Carboxylic ester hydrolase, single mutant h48n of bovine pancreatic pla2 enzyme

spinqualitylabelsall models 2zp4, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zp4 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL, MRD Related: 2zp3, 2zp5 Gene: PLA2G1B (Bos taurus) Activity: Phospholipase A(2), with EC number 3.1.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PA21B_BOVIN] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. 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 Phospholipase A(2) hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A(2). To elucidate the structural role of His48 and Asp49, the crystal structures of three active-site single mutants H48N, D49N and D49K have been determined at 1.9 A resolution. Although the catalytically important calcium ion is present in the H48N mutant, the crystal structure shows that proton transfer is not possible from the catalytic water to the mutated residue. In the case of the Asp49 mutants, no calcium ion was found in the active site. However, the tertiary structures of the three active-site mutants are similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation studies provide a good explanation for the crystallographic results. Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2).,Kanaujia SP, Sekar K Acta Crystallogr D Biol Crystallogr. 2008 Oct;64(Pt 10):1003-11. Epub 2008, Sep 19. PMID:18931407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A2

Proteopedia Page Contributors and Editors (what is this?)

OCA