1crl
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1crl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crl OCA], [http://www.ebi.ac.uk/pdbsum/1crl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1crl RCSB]</span> | ||
}} | }} | ||
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[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
[[Category: Grochulski, P.]] | [[Category: Grochulski, P.]] | ||
| - | [[Category: NAG]] | ||
[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic esterase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:27:14 2008'' |
Revision as of 16:27, 30 March 2008
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| , resolution 2.06Å | |||||||
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| Ligands: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE
Overview
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 Structure
1CRL is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
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:8509417
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