1REO

L-amino acid oxidase from Agkistrodon halys pallas

1REO の概要

• エントリーDOI: 10.2210/pdb1reo/pdb
• 分子名称: AHPLAAO, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRIC ACID, ... (5 entities in total)
• 機能のキーワード: l-amino acid oxidase, oxidoreductase
• 由来する生物種: Gloydius halys (halys viper)
• 細胞内の位置: Secreted: Q6STF1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56627.29

構造登録者

Zhang, H.,Teng, M.,Niu, L.,Wang, Y.,Wang, Y.,Liu, Q.,Huang, Q.,Hao, Q.,Dong, Y.,Liu, P. (登録日: 2003-11-07, 公開日: 2004-05-04, 最終更新日: 2024-10-30)

主引用文献

Zhang, H.,Teng, M.,Niu, L.,Wang, Y.,Wang, Y.,Liu, Q.,Huang, Q.,Hao, Q.,Dong, Y.,Liu, P.
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.
Acta Crystallogr.,Sect.D, 60:974-977, 2004

PubMed Abstract: 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.

PubMed: 15103157
DOI: 10.1107/S0907444904000046

実験手法

X-RAY DIFFRACTION (2.31 Å)