2ph4: Difference between revisions

Revision as of 10:06, 28 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:2ph4.png

Template:STRUCTURE 2ph4

Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venomCrystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom

Template:ABSTRACT PUBMED 18295812

About this StructureAbout this Structure

2PH4 is a Single protein structure of sequence from Zhaoermia mangshanensis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a novel myotoxic Arg49 phospholipase A(2) homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: Insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus., Murakami MT, Kuch U, Betzel C, Mebs D, Arni RK, Toxicon. 2008 Apr;51(5):723-35. Epub 2007 Nov 29. PMID:18295812

Page seeded by OCA on Mon Jul 28 10:06:00 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ph4.jpg|left|200px]]
+{{Seed}}
+[[Image:2ph4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ph4|  PDB=2ph4  |  SCENE=  }}
-'''Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom'''
+===Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom===
-==Overview==
+<!--
-The venom of Zhaoermia mangshanensis, encountered solely in Mt Mang in China's Hunan Province, exhibits coagulant, phosphodiesterase, l-amino acid oxidase, kallikrein, phospholipase A(2) and myotoxic activities. The catalytically inactive PLA(2) homolog referred to as zhaoermiatoxin is highly myotoxic and displays high myonecrotic and edema activities. Zhaoermiatoxin possesses a molecular weight of 13,972Da, consists of 121 amino-acid residues cross-linked by seven disulfide bridges and shares high sequence homology with Lys49-PLA(2)s from the distantly related Asian pitvipers. However, zhaoermiatoxin possesses an arginine residue at position 49 instead of a lysine, thereby suggesting a secondary Lys49--&gt;Arg substitution which results in a catalytically inactive protein. We have determined the first crystal structure of zhaoermiatoxin, an Arg49-PLA(2), from Zhaoermia mangshanensis venom at 2.05A resolution, which represents a novel member of phospholipase A(2) family. In this structure, unlike the Lys49 PLA(2)s, the C-terminus is well ordered and an unexpected non-polarized state of the putative calcium-binding loop due to the flip of Lys122 towards the bulk solvent is observed. The orientation of the Arg-49 side chain results in a similar binding mode to that observed in the Lys49 PLA(2)s; however, the guadinidium group is tri-coordinated by carbonyl oxygen atoms of the putative calcium-binding loop, whereas the Nzeta atom of lysine is tetra-coordinated as a result of the different conformation adopted by the putative calcium-binding loop.
+The line below this paragraph, {{ABSTRACT_PUBMED_18295812}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18295812 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18295812}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Phospholipase a2]]
 [[Category: Snake venom]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:07:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:06:00 2008''