1OP2

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

Summary for 1OP2

• Entry DOI: 10.2210/pdb1op2/pdb
• Related: 1OP0
• Descriptor: Venom serine proteinase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: snake venom, serine proteinase, glycoprotein, agkistrodon acutus, hydrolase
• Biological source: Deinagkistrodon acutus (Chinese moccasin)
• Cellular location: Secreted: Q9I8X1
• Total number of polymer chains: 1
• Total formula weight: 25673.96

Authors

Zhu, Z.,Teng, M.,Niu, L. (deposition date: 2003-03-04, release date: 2004-05-25, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)