1u4j: Difference between revisions

Revision as of 12:15, 27 July 2008

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File:1u4j.png

Template:STRUCTURE 1u4j

Crystal structure of a carbohydrate induced dimer of group I phospholipase A2 from Bungarus caeruleus at 2.1 A resolutionCrystal structure of a carbohydrate induced dimer of group I phospholipase A2 from Bungarus caeruleus at 2.1 A resolution

Template:ABSTRACT PUBMED 15721580

About this StructureAbout this Structure

1U4J is a Single protein structure of sequence from Bungarus caeruleus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a carbohydrate induced homodimer of phospholipase A2 from Bungarus caeruleus at 2.1A resolution., Singh G, Gourinath S, Sarvanan K, Sharma S, Bhanumathi S, Betzel Ch, Yadav S, Srinivasan A, Singh TP, J Struct Biol. 2005 Mar;149(3):264-72. PMID:15721580

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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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 {{STRUCTURE_1u4j|  PDB=1u4j  |  SCENE=  }}
-'''Crystal structure of a carbohydrate induced dimer of group I phospholipase A2 from Bungarus caeruleus at 2.1 A resolution'''
+===Crystal structure of a carbohydrate induced dimer of group I phospholipase A2 from Bungarus caeruleus at 2.1 A resolution===
-==Overview==
+<!--
-This is the first crystal structure of a carbohydrate induced dimer of phospholipase A(2) (PLA(2)). This is an endogenous complex formed between two PLA(2) molecules and two mannoses. It was isolated from Krait venom (Bungarus caeruleus) and crystallized as such. The complete amino acid sequence of PLA(2) was determined using cDNA method. Three-dimensional structure of the complex has been solved with molecular replacement method and refined to a final R-factor of 0.192 for all the data in the resolution range 20.0-2.1A. The presence of mannose molecules in the protein crystals was confirmed using dinitrosalicylic acid test and the molecular weight of the dimer was verified with MALDI-TOF. As indicated by dynamic light scattering and analytical ultracentrifugation the dimer was also stable in solution. The good quality non-protein electron density at the interface of two PLA(2) molecules enabled us to model two mannoses. The mannoses are involved extensively in interactions with protein atoms of both PLA(2) molecules. Some of the critical amino acid residues such as Asp 49 and Tyr 31, which are part of the substrate-binding site, are found facing the interface and interacting with mannoses. The structure of the complex clearly shows that the dimerization is caused by mannoses and it results in the loss of enzymatic activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15721580}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15721580 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15721580}}
 ==About this Structure==
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 [[Category: Mannose]]
 [[Category: Phospholipase a2]]
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