Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2W22

Activation Mechanism of Bacterial Thermoalkalophilic Lipases

2W22 の概要
エントリーDOI10.2210/pdb2w22/pdb
分子名称TRIACYLGLYCEROL LIPASE, CALCIUM ION, ZINC ION, ... (6 entities in total)
機能のキーワードthermoalkalophilic lipases, hydrolase, open conformation, activation mechanism
由来する生物種GEOBACILLUS THERMOCATENULATUS
タンパク質・核酸の鎖数1
化学式量合計45034.00
構造登録者
Carrasco-Lopez, C.,Godoy, C.,De Las Rivas, B.,Fernandez-Lorente, G.,Palomo, J.M.,Guisan, J.M.,Fernandez-Lafuente, R.,Hermoso, J.A. (登録日: 2008-10-23, 公開日: 2008-12-16, 最終更新日: 2023-12-13)
主引用文献Carrasco-Lopez, C.,Godoy, C.,de Las Rivas, B.,Fernandez-Lorente, G.,Palomo, J.M.,Guisan, J.M.,Fernandez-Lafuente, R.,Martinez-Ripoll, M.,Hermoso, J.A.
Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements.
J. Biol. Chem., 284:4365-4372, 2009
Cited by
PubMed Abstract: The bacterial thermoalkalophilic lipases that hydrolyze saturated fatty acids at 60-75 degrees C and pH 8-10 are grouped as the lipase family I.5. We report here the crystal structure of the lipase from Geobacillus thermocatenulatus, the first structure of a member of the lipase family I.5 showing an open configuration. Unexpectedly, enzyme activation involves large structural rearrangements of around 70 amino acids and the concerted movement of two lids, the alpha6- and alpha7-helices, unmasking the active site. Central in the restructuring process of the lids are both the transfer of bulky hydrophobic residues out of the N-terminal end of the alpha6-helix and the incorporation of short side chain residues to the alpha6 C-terminal end. All these structural changes are stabilized by the Zn(2+)-binding domain, which is characteristic of this family of lipases. Two detergent molecules are placed in the active site, mimicking chains of the triglyceride substrate, demonstrating the position of the oxyanion hole and the three pockets that accommodate the sn-1, sn-2, and sn-3 fatty acids chains. The combination of structural and biochemical studies indicate that the lid opening is not mediated by temperature but triggered by interaction with lipid substrate.
PubMed: 19056729
DOI: 10.1074/jbc.M808268200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 2w22
検証レポート(詳細版)ダウンロードをダウンロード

235666

件を2025-05-07に公開中

PDB statisticsPDBj update infoContact PDBjnumon