1tia
From Proteopedia
(New page: 200px<br /><applet load="1tia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tia, resolution 2.1Å" /> '''AN UNUSUAL BURIED POL...) |
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| - | [[Image:1tia.gif|left|200px]]<br /><applet load="1tia" size=" | + | [[Image:1tia.gif|left|200px]]<br /><applet load="1tia" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tia, resolution 2.1Å" /> | caption="1tia, resolution 2.1Å" /> | ||
'''AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES'''<br /> | '''AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The stability of globular proteins arises largely from the burial of | + | The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. 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:// | + | 1TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. 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=1TIA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
| - | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
[[Category: Swenson, L.]] | [[Category: Swenson, L.]] | ||
[[Category: Wei, Y.]] | [[Category: Wei, Y.]] | ||
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[[Category: hydrolase(carboxylic esterase)]] | [[Category: hydrolase(carboxylic esterase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:47 2008'' |
Revision as of 13:13, 21 February 2008
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AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES
Overview
The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis.
About this Structure
1TIA is a Single protein structure of sequence from Penicillium camemberti. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
An unusual buried polar cluster in a family of fungal lipases., Derewenda U, Swenson L, Green R, Wei Y, Dodson GG, Yamaguchi S, Haas MJ, Derewenda ZS, Nat Struct Biol. 1994 Jan;1(1):36-47. PMID:7656005
Page seeded by OCA on Thu Feb 21 15:13:47 2008
