Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound states

Murakami, M. T.Gabdoulkhakov, A.Genov, N.Cintra, A. C. O.Betzel, C.Arni, R. K.2014-05-202014-05-202006-05-01Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 88, n. 5, p. 543-549, 2006.0300-9084http://hdl.handle.net/11449/21958The electrophile Ca2+ is an essential multifunctional co-factor in the phospholipase A(2) mediated hydrolysis of phospholipids. Crystal structures of an acidic phospholipase A(2) from the venom of Bothrops jararacussu have been determined both in the Ca2+ free and bound states at 0.97 and 1.60 angstrom resolutions, respectively. In the Ca2+ bound state, the Ca2+ ion is penta-coordinated by a distorted pyramidal cage of oxygen and nitrogen atoms that is significantly different to that observed in structures of other Group I/II phospholipases A(2). In the absence of Ca2+, a water molecule occupies the position of the Ca2+ ion and the side chain of Asp49 and the calcium-binding loop adopts a different conformation. (c) 2005 Elsevier SAS. All rights reserved.543-549engsnake venomphospholipase A(2)Ca2+ coordinationanticoagulant activityX-ray analysisInsights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound statesArtigo10.1016/j.biochi.2005.10.014WOS:000239270500015Acesso restrito91625089789458870000-0003-2460-1145