1pc9
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| , resolution 2.5Å | |||||||
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| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Related: | 1PA0
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of BnSP-6, a Lys49-Phospholipase A2
OverviewOverview
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 StructureAbout this Structure
1PC9 is a Single protein structure of sequence from Bothrops neuwiedi pauloensis. Full crystallographic information is available from OCA.
ReferenceReference
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
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