1OP2

Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus

1OP2 の概要

• エントリーDOI: 10.2210/pdb1op2/pdb
• 関連するPDBエントリー: 1OP0
• 分子名称: Venom serine proteinase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: snake venom, serine proteinase, glycoprotein, agkistrodon acutus, hydrolase
• 由来する生物種: Deinagkistrodon acutus (Chinese moccasin)
• 細胞内の位置: Secreted: Q9I8X1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25673.96

構造登録者

Zhu, Z.,Teng, M.,Niu, L. (登録日: 2003-03-04, 公開日: 2004-05-25, 最終更新日: 2024-10-23)

主引用文献

Zhu, Z.,Liang, Z.,Zhang, T.,Zhu, Z.,Xu, W.,Teng, M.,Niu, L.
Crystal Structures and Amidolytic Activities of Two Glycosylated Snake Venom Serine Proteinases
J.BIOL.CHEM., 280:10524-10529, 2005

PubMed Abstract: We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.

PubMed: 15632114
DOI: 10.1074/jbc.M412900200

実験手法

X-RAY DIFFRACTION (2.1 Å)