2lip

From Proteopedia

Revision as of 15:30, 30 October 2007

PSEUDOMONAS LIPASE OPEN CONFORMATION

Overview

BACKGROUND:. 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). ... [(full description)]

About this Structure

2LIP is a [Single protein] structure of sequence from [Burkholderia cepacia] with CA as [ligand]. Active as [Triacylglycerol lipase], with EC number [3.1.1.3]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

The open conformation of a Pseudomonas lipase., Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A, Structure. 1997 Feb 15;5(2):187-202. PMID:9032074

Page seeded by OCA on Tue Oct 30 17:35:40 2007