1tia

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{{STRUCTURE_1tia| PDB=1tia | SCENE= }}
{{STRUCTURE_1tia| PDB=1tia | SCENE= }}
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'''AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES'''
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===AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_7656005}}
==About this Structure==
==About this Structure==
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[[Category: Wei, Y.]]
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[[Category: Yamaguchi, S.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:58:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:18:41 2008''

Revision as of 20:18, 28 July 2008

Image:1tia.png

Template:STRUCTURE 1tia

AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES

Template:ABSTRACT PUBMED 7656005

About this Structure

1TIA is a Single protein structure of sequence from Penicillium camemberti. 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 Mon Jul 28 23:18:41 2008

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