1pa0: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND=  
|LIGAND=  
|ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pa0 OCA], [http://www.ebi.ac.uk/pdbsum/1pa0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pa0 RCSB]</span>
}}
}}


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[[Category: myotoxin]]
[[Category: myotoxin]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:00 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:56:59 2008''

Revision as of 22:57, 30 March 2008

File:1pa0.jpg


PDB ID 1pa0

Drag the structure with the mouse to rotate
, resolution 2.20Å
Activity: Phospholipase A(2), with EC number 3.1.1.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BNSP-7, 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

1PA0 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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