1pob | pdb_00001pob
CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE
Structural highlights
FunctionPA2A1_NAJAT Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2] 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 PubMedThe crystal structure of a complex between a phosphonate transition-state analogue and the phospholipase A2 (PLA2) from Naja naja atra venom has been solved and refined to a resolution of 2.0 angstroms. The identical stereochemistry of the two complexes that comprise the crystal's asymmetric unit indicates both the manner in which the transition state is stabilized and how the hydrophobic fatty acyl chains of the substrate are accommodated by the enzyme during interfacial catalysis. The critical features that suggest the chemistry of binding and catalysis are the same as those seen in the crystal structure of a similar complex formed with the evolutionarily distant bee-venom PLA2. Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue.,White SP, Scott DL, Otwinowski Z, Gelb MH, Sigler PB Science. 1990 Dec 14;250(4987):1560-3. PMID:2274787[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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