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

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorMurakami, M. T.
dc.creatorGabdoulkhakov, A.
dc.creatorGenov, N.
dc.creatorCintra, A. C. O.
dc.creatorBetzel, C.
dc.creatorArni, R. K.
dc.date2014-05-20T14:02:18Z
dc.date2016-10-25T17:09:01Z
dc.date2014-05-20T14:02:18Z
dc.date2016-10-25T17:09:01Z
dc.date2006-05-01
dc.date.accessioned2017-04-05T21:27:11Z
dc.date.available2017-04-05T21:27:11Z
dc.identifierBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 88, n. 5, p. 543-549, 2006.
dc.identifier0300-9084
dc.identifierhttp://hdl.handle.net/11449/21958
dc.identifierhttp://acervodigital.unesp.br/handle/11449/21958
dc.identifier10.1016/j.biochi.2005.10.014
dc.identifierWOS:000239270500015
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2005.10.014
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/867436
dc.descriptionThe 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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimie
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectsnake venom
dc.subjectphospholipase A(2)
dc.subjectCa2+ coordination
dc.subjectanticoagulant activity
dc.subjectX-ray analysis
dc.titleInsights 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
dc.typeOtro


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