2LIP

PSEUDOMONAS LIPASE OPEN CONFORMATION

2LIP の概要

• エントリーDOI: 10.2210/pdb2lip/pdb
• 分子名称: LIPASE, CALCIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, lipase, pseudomonas, catalytic triad
• 由来する生物種: Burkholderia cepacia
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33190.84

構造登録者

Schrag, J.D.,Cygler, M. (登録日: 1996-12-13, 公開日: 1997-03-12, 最終更新日: 2024-10-23)

主引用文献

Schrag, J.D.,Li, Y.,Cygler, M.,Lang, D.,Burgdorf, T.,Hecht, H.J.,Schmid, R.,Schomburg, D.,Rydel, T.J.,Oliver, J.D.,Strickland, L.C.,Dunaway, C.M.,Larson, S.B.,Day, J.,McPherson, A.
The open conformation of a Pseudomonas lipase.
Structure, 5:187-202, 1997

PubMed Abstract: . The interfacial activation of lipases results primarily from conformational changes in the enzymes which expose the active site and provide a hydrophobic surface for interaction with the lipid substrate. Comparison of the crystallization conditions used and the structures observed for a variety of lipases suggests that the enzyme conformation is dependent on solution conditions. Pseudomonas cepacia lipase (PCL) was crystallized in conditions from which the open, active conformation of the enzyme was expected. Its three-dimensional structure was determined independently in three different laboratories and was compared with the previously reported closed conformations of the closely related lipases from Pseudomonas glumae (PGL) and Chromobacterium viscosum (CVL). These structures provide new insights into the function of this commercially important family of lipases.

PubMed: 9032074
DOI: 10.1016/S0969-2126(97)00178-0

実験手法

X-RAY DIFFRACTION (2.1 Å)