1crl: Difference between revisions

New page: left|200px<br /><applet load="1crl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1crl, resolution 2.06Å" /> '''INSIGHTS INTO INTERF...
 
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[[Image:1crl.gif|left|200px]]<br /><applet load="1crl" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1crl.gif|left|200px]]<br /><applet load="1crl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1crl, resolution 2.06&Aring;" />
caption="1crl, resolution 2.06&Aring;" />
'''INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE'''<br />
'''INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE'''<br />


==Overview==
==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.
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==
==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 NAG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CRL OCA].  
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].  


==Reference==
==Reference==
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[[Category: hydrolase(carboxylic esterase)]]
[[Category: hydrolase(carboxylic esterase)]]


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