1IJL

Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus

Summary for 1IJL

• Entry DOI: 10.2210/pdb1ijl/pdb
• Related: 1PSJ
• Descriptor: PHOSPHOLIPASE A2, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: three long helix, one two strand beta sheet, calcium binding loop, hydrolase
• Biological source: Deinagkistrodon acutus (Chinese moccasin)
• Cellular location: Secreted: Q7SID6
• Total number of polymer chains: 2
• Total formula weight: 28328.92

Authors

Gu, L.,Zhang, H.,Song, S.,Zhou, Y.,Lin, Z. (deposition date: 2001-04-27, release date: 2001-12-28, Last modification date: 2024-10-16)

Primary citation

Gu, L.,Zhang, H.,Song, S.,Zhou, Y.,Lin, Z.
Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.
Acta Crystallogr.,Sect.D, 58:104-110, 2002

PubMed Abstract: An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.

PubMed: 11752784
DOI: 10.1107/S0907444901018170

Experimental method

X-RAY DIFFRACTION (2.6 Å)