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1pc9
From Proteopedia
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Crystal Structure of BnSP-6, a Lys49-Phospholipase A2
Overview
Phospholipases A(2) are components of Bothrops venoms responsible for, disruption of cell membrane integrity via hydrolysis of its phospholipids., A class of PLA(2)-like proteins has been described which despite PLA(2), activity on artificial substrate, due to a D49K mutation, is still highly, myonecrotic. This work reports the X-ray structure determination of two, Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This, comparison reveals that there are not just two ("open" and "closed") but, at least six different conformations. The binding of fatty acid observed, in three recent Lys49-PLA(2) structures seems to be independent of their, quaternary conformation. Cys29 polarization by Lys122 is not significant, for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These, structures may be in an "active" state when nothing is bound to them and, the Lys122/Cys29 interactions are weak or absent.
About this Structure
1PC9 is a Single protein structure of sequence from Bothrops neuwiedi pauloensis. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights., Magro AJ, Soares AM, Giglio JR, Fontes MR, Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331
Page seeded by OCA on Tue Nov 20 23:40:53 2007
