1lpn

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[[Image:1lpn.jpg|left|200px]]<br /><applet load="1lpn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lpn.jpg|left|200px]]
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caption="1lpn, resolution 2.18&Aring;" />
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'''ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE'''<br />
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{{Structure
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|PDB= 1lpn |SIZE=350|CAPTION= <scene name='initialview01'>1lpn</scene>, resolution 2.18&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=DSC:DODECANESULFONATE ION'>DSC</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LPN 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=DSC:'>DSC</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=1LPN OCA].
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1LPN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPN OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8142346 8142346]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8142346 8142346]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Triacylglycerol lipase]]
[[Category: Triacylglycerol lipase]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:40 2008''

Revision as of 10:33, 20 March 2008

Image:1lpn.jpg


PDB ID 1lpn

Drag the structure with the mouse to rotate
, resolution 2.18Å
Ligands: , and
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Coordinates: save as pdb, mmCIF, xml



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


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.

About this Structure

1LPN is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

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 Mar 20 12:33:40 2008

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