3lip
From Proteopedia
(New page: 200px<br /> <applet load="3lip" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lip, resolution 2.0Å" /> '''OPEN CONFORMATION OF...) |
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==About this Structure== | ==About this Structure== | ||
| - | 3LIP 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3LIP OCA]]. | + | 3LIP 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 Sites: ACT and OXY. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3LIP OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: without inhibitor]] | [[Category: without inhibitor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:34:59 2007'' |
Revision as of 06:30, 30 October 2007
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OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
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
3LIP is a [Single protein] structure of sequence from [Burkholderia cepacia] with CA as [ligand]. Active as [Hydrolase], with EC number [3.1.1.3]. Structure known Active Sites: ACT and OXY. 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
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