1qll: Difference between revisions

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[[Image:1qll.gif|left|200px]]
[[Image:1qll.gif|left|200px]]


{{Structure
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|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>
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{{STRUCTURE_1qll| PDB=1qll  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qll OCA], [http://www.ebi.ac.uk/pdbsum/1qll PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qll RCSB]</span>
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'''PIRATOXIN-II (PRTX-II)-A K49 PLA2 FROM BOTHROPS PIRAJAI'''
'''PIRATOXIN-II (PRTX-II)-A K49 PLA2 FROM BOTHROPS PIRAJAI'''
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Structural basis for low catalytic activity in Lys49 phospholipases A2--a hypothesis: the crystal structure of piratoxin II complexed to fatty acid., Lee WH, da Silva Giotto MT, Marangoni S, Toyama MH, Polikarpov I, Garratt RC, Biochemistry. 2001 Jan 9;40(1):28-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11141053 11141053]
Structural basis for low catalytic activity in Lys49 phospholipases A2--a hypothesis: the crystal structure of piratoxin II complexed to fatty acid., Lee WH, da Silva Giotto MT, Marangoni S, Toyama MH, Polikarpov I, Garratt RC, Biochemistry. 2001 Jan 9;40(1):28-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11141053 11141053]
[[Category: Bothrops pirajai]]
[[Category: Bothrops pirajai]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lee, W H.]]
[[Category: Lee, W H.]]
[[Category: Polikarpov, I.]]
[[Category: Polikarpov, I.]]
[[Category: k49 phospholipase a2 (pla2)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:25:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:26 2008''

Revision as of 06:25, 3 May 2008

File:1qll.gif

Template:STRUCTURE 1qll

PIRATOXIN-II (PRTX-II)-A K49 PLA2 FROM BOTHROPS PIRAJAI


OverviewOverview

Asp49 plays a fundamental role in supporting catalysis by phospholipases A2 by coordinating the calcium ion which aids in the stabilization of the tetrahedral intermediate. In several myotoxins from the venoms of Viperidae snakes, this aspartic acid is substituted by lysine. The loss of calcium binding capacity by these mutants has become regarded as the standard explanation for their greatly reduced or nonexistent phospholipolytic activity. Here we describe the crystal structure of one such Lys49 PLA2, piratoxin-II, in which a fatty acid molecule is observed within the substrate channel. This suggests that such toxins may be active enzymes in which catalysis is interrupted at the stage of substrate release. Comparison of the present structure with other PLA2s, both active and inactive, identifies Lys122 as one of the likely causes of the increased affinity for fatty acid in Lys49 enzymes. Its interaction with the mainchain carbonyl of Cys29 is expected to lead to hyperpolarization of the peptide bond between residues 29 and 30 leading to an increased affinity for the fatty acid headgroup. This strongly bound fatty acid may serve as an anchor to secure the toxin within the membrane thus facilitating its pathological effects.

About this StructureAbout this Structure

1QLL is a Single protein structure of sequence from Bothrops pirajai. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for low catalytic activity in Lys49 phospholipases A2--a hypothesis: the crystal structure of piratoxin II complexed to fatty acid., Lee WH, da Silva Giotto MT, Marangoni S, Toyama MH, Polikarpov I, Garratt RC, Biochemistry. 2001 Jan 9;40(1):28-36. PMID:11141053 Page seeded by OCA on Sat May 3 06:25:12 2008

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