1qll: Difference between revisions

Revision as of 13:13, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qll.png

Template:STRUCTURE 1qll

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

Template:ABSTRACT PUBMED 11141053

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''PIRATOXIN-II (PRTX-II)-A K49 PLA2 FROM BOTHROPS PIRAJAI'''
+===PIRATOXIN-II (PRTX-II)-A K49 PLA2 FROM BOTHROPS PIRAJAI===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11141053}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11141053}}
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 [[Category: Lee, W H.]]
 [[Category: Polikarpov, I.]]
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