2lip

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
==About this Structure==
==About this Structure==
-
2LIP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LIP OCA]].
+
2LIP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LIP OCA]].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Burkholderia cepacia]]
[[Category: Burkholderia cepacia]]
[[Category: Single protein]]
[[Category: Single protein]]
 +
[[Category: Triacylglycerol lipase]]
[[Category: Cygler, M.]]
[[Category: Cygler, M.]]
[[Category: Schrag, J.D.]]
[[Category: Schrag, J.D.]]
Line 22: Line 23:
[[Category: pseudomonas]]
[[Category: pseudomonas]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:34:54 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:33:52 2007''

Revision as of 08:29, 30 October 2007


2lip, resolution 2.1Å

Drag the structure with the mouse to rotate

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 10:33:52 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools