1lpp: Difference between revisions

Revision as of 14:47, 21 February 2008

ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

OverviewOverview

The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a "tuning fork" conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.

About this StructureAbout this Structure

1LPP is a Single protein structure of sequence from [1] with , and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.

ReferenceReference

Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase., Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M, Biochemistry. 1994 Mar 29;33(12):3494-500. PMID:8142346

Page seeded by OCA on Thu Feb 21 13:47:14 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1lpp.jpg|left|200px]]<br /><applet load="1lpp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lpp.jpg|left|200px]]<br /><applet load="1lpp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lpp, resolution 2.18&Aring;" />
 '''ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE'''<br />
 ==Overview==
-The structures of Candida rugosa lipase-inhibitor complexes demonstrate, that the scissile fatty acyl chain is bound in a narrow, hydrophobic, tunnel which is unique among lipases studied to date. Modeling of, triglyceride binding suggests that the bound lipid must adopt a "tuning, fork" conformation. The complexes, analogs of tetrahedral intermediates of, the acylation and deacylation steps of the reaction pathway, localize the, components of the oxyanion hole and define the stereochemistry of ester, hydrolysis. Comparison with other lipases suggests that the positioning of, the scissile fatty acyl chain and ester bond and the stereochemistry of, hydrolysis are the same in all lipases which share the, alpha/beta-hydrolase fold.
+The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a "tuning fork" conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.
 ==About this Structure==
-LPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NAG, CA and HDS as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LPP OCA].
+LPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HDS:'>HDS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPP OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Triacylglycerol lipase]]
-[[Category: Cygler, M.C.]]
+[[Category: Cygler, M C.]]
-[[Category: Grochulski, P.G.]]
+[[Category: Grochulski, P G.]]
 [[Category: CA]]
 [[Category: HDS]]
@@ Line 20: / Line 20: @@
 [[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:46:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:14 2008''