1A3D

PHOSPHOLIPASE A2 (PLA2) FROM NAJA NAJA VENOM

1A3D の概要

• エントリーDOI: 10.2210/pdb1a3d/pdb
• 分子名称: PHOSPHOLIPASE A2, SODIUM ION (3 entities in total)
• 機能のキーワード: phospholipase, trimer, calcium binding, activator site, carboxylic ester hydrolase
• 由来する生物種: Naja naja (Indian cobra)
• 細胞内の位置: Secreted: P15445
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13380.84

構造登録者

Segelke, B.W.,Nguyen, D.,Chee, R.,Xuong, H.N.,Dennis, E.A. (登録日: 1998-01-20, 公開日: 1998-04-29, 最終更新日: 2024-10-23)

主引用文献

Segelke, B.W.,Nguyen, D.,Chee, R.,Xuong, N.H.,Dennis, E.A.
Structures of two novel crystal forms of Naja naja naja phospholipase A2 lacking Ca2+ reveal trimeric packing.
J.Mol.Biol., 279:223-232, 1998

PubMed Abstract: Three crystal forms of Naja naja naja phospholipase A2 were discovered through random crystallization screening, including two heretofore uncharacterized forms. The crystallization conditions for both of these novel crystal forms are Ca(2+)-free whereas previously reported conditions include Ca2+. One of the new crystal forms has a cubic lattice in the space group P2(1)3 (a = b = c = 69.24 A), the other has an orthorhombic lattice in the space group P2(1)2(1)2(1) (a = 67.22 A, b = 73.48 A, c = 87.52 A) and a previously characterized crystal belong to the tetragonal space group P4(3)2(1)2 (a = b = 88.6 A, c = 107.4 A). The structure from the cubic crystal form has been determined to 1.8 A and refined to an R-factor of 17% while the structure from the orthorhombic form has been determined to 2.65 A and has been refined to an R-factor of 21%. The determination of the cubic structure extends the resolution to which structures of this molecule have been determined from 2.3 A to 1.8 A. The two newly determined structures, in combination with the previously determined structure, generate an informative structural ensemble from which structural changes due to Ca2+, which is required for catalysis, and the effect of crystal contacts on side-chain conformations and oligomeric association can be inferred. Both of the newly determined structures reveal a trimeric oligomer as observed in the tetragonal structure; this appears to be a unique feature of the Naja naja naja enzyme.

PubMed: 9636712
DOI: 10.1006/jmbi.1998.1759

実験手法

X-RAY DIFFRACTION (1.8 Å)