1PC9

Crystal Structure of BnSP-6, a Lys49-Phospholipase A2

Summary for 1PC9

• Entry DOI: 10.2210/pdb1pc9/pdb
• Related: 1PA0
• Descriptor: BnSP-6 (2 entities in total)
• Functional Keywords: lys49-phospholipase a2, myotoxin, bothrops, venom., hydrolase
• Biological source: Bothrops neuwiedi pauloensis
• Cellular location: Secreted: Q9IAT9
• Total number of polymer chains: 2
• Total formula weight: 27362.02

Authors

Magro, A.J.,Soares, A.M.,Giglio, J.R.,Fontes, M.R.M. (deposition date: 2003-05-16, release date: 2004-06-01, Last modification date: 2024-04-03)

Primary citation

Magro, A.J.,Soares, A.M.,Giglio, J.R.,Fontes, M.R.M.
Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights.
Biochem.Biophys.Res.Commun., 311:713-720, 2003

PubMed Abstract: 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.

PubMed: 14623331
DOI: 10.1016/j.bbrc.2003.10.047

Experimental method

X-RAY DIFFRACTION (2.5 Å)