1crl: Difference between revisions

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[[Image:1crl.gif|left|200px]]<br /><applet load="1crl" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1crl.gif|left|200px]]
caption="1crl, resolution 2.06&Aring;" />
 
'''INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE'''<br />
{{Structure
|PDB= 1crl |SIZE=350|CAPTION= <scene name='initialview01'>1crl</scene>, resolution 2.06&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|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]
|GENE=
}}
 
'''INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1CRL 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> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRL OCA].  
1CRL 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=1CRL OCA].  


==Reference==
==Reference==
Insights into interfacial activation from an open structure of Candida rugosa lipase., Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M, J Biol Chem. 1993 Jun 15;268(17):12843-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8509417 8509417]
Insights into interfacial activation from an open structure of Candida rugosa lipase., Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M, J Biol Chem. 1993 Jun 15;268(17):12843-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8509417 8509417]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Triacylglycerol lipase]]
[[Category: Triacylglycerol lipase]]
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[[Category: hydrolase(carboxylic esterase)]]
[[Category: hydrolase(carboxylic esterase)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:02 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:03 2008''

Revision as of 11:28, 20 March 2008

File:1crl.gif


PDB ID 1crl

Drag the structure with the mouse to rotate
, resolution 2.06Å
Ligands:
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Coordinates: save as pdb, mmCIF, xml



INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE


OverviewOverview

The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site. Comparison with the crystal structure of the homologous lipase from Geotrichum candidum, in which the active site is covered by surface loops and is inaccessible from the solvent, shows that the largest structural differences occur in the vicinity of the active site. Three loops in this region differ significantly in conformation, and the interfacial activation of these lipases is likely to be associated with conformational rearrangements of these loops. The "open" structure provides a new image of the substrate binding region and active site access, which is different from that inferred from the structure of the "closed" form of the G. candidum lipase.

About this StructureAbout this Structure

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

ReferenceReference

Insights into interfacial activation from an open structure of Candida rugosa lipase., Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M, J Biol Chem. 1993 Jun 15;268(17):12843-7. PMID:8509417

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