1zlb
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(New page: 200px<br /><applet load="1zlb" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zlb, resolution 0.97Å" /> '''Crystal structure of...)
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Revision as of 15:37, 29 January 2008
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Crystal structure of catalytically-active phospholipase A2 in the absence of calcium
Overview
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.
About this Structure
1ZLB is a Single protein structure of sequence from Bothrops jararacussu. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
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., Murakami MT, Gabdoulkhakov A, Genov N, Cintra AC, Betzel C, Arni RK, Biochimie. 2006 May;88(5):543-9. Epub 2005 Dec 5. PMID:16376474
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