1reo

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Revision as of 23:24, 20 November 2007

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spinqualitylabelsall models 1reo, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

L-amino acid oxidase from Agkistrodon halys pallas

Overview

A snake-venom protein named AHP-LAAO has been purified from Agkistrodon, halys pallas venom using four-stage chromatography. AHP-LAAO is a novel, member of the snake-venom L-amino-acid oxidase family. Its amino-acid, sequence shows high homology to other members of this family. For, L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as, determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce, apoptosis of cultured Hela cells. Two sets of diffraction data with, similar resolution limits (about 2.5 A) were collected independently at, MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute, of High Energy Physics, Beijing, China). The crystals belong to space, group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one, molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3), Da(-1). The final structural model is similar to that of L-amino-acid, oxidase from Calloselasma rhodostoma venom.

About this Structure

1REO is a Single protein structure of sequence from Gloydius halys with NAG, NDG, CIT and FAD as ligands. Active as L-amino-acid oxidase, with EC number 1.4.3.2 Full crystallographic information is available from OCA.

Reference

Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom., Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):974-7. Epub 2004, Apr 21. PMID:15103157

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