Insights into metal ion binding in phospholipases A2: ultra high-resolution crystal structures of an acidic phospholipase A2 in the Ca2+ free and bound states |
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| Authors: | Murakami M T Gabdoulkhakov A Genov N Cintra A C O Betzel C Arni R K |
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| Institution: | 1. Department of Physics, IBILCE/UNESP, Cristovão Colombo 2265, São José do Rio Preto, SP 15054-000, Brazil;2. Institute of Protein Research RAS, Puschino, Moscow Region 142290, Russia;3. Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria;4. Department of Biochemistry, USP, Ribeirão Preto 14040902, Brazil;5. Institute of Medical Biochemistry and Molecular Biology, 22603 Hamburg, Germany;6. Center for Applied Toxinology, Butantan Institute, São Paulo 05503900, Brazil |
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| Abstract: | The electrophile Ca(2+) 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 Ca(2+) free and bound states at 0.97 and 1.60 A resolutions, respectively. In the Ca(2+) bound state, the Ca(2+) 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 Ca(2+), a water molecule occupies the position of the Ca(2+) ion and the side chain of Asp49 and the calcium-binding loop adopts a different conformation. |
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| Keywords: | Snake venom Phospholipases A2 Ca2+ coordination Anticoagulant activity X-ray analysis |
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