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Crystal structure of a carbohydrate induced homodimer of phospholipase A2 from Bungarus caeruleus at 2.1A resolution.

Abstract：

: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.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Singh G,Gourinath S,Sarvanan K,Sharma S,Bhanumathi S,Betzel Ch,Yadav S,Srinivasan A,Singh TP

doi

10.1016/j.jsb.2004.11.011

keywords:

subject

Has Abstract

pub_date

2005-03-01 00:00:00

pages

264-72

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(04)00221-7

journal_volume

149

pub_type

杂志文章

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