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1tia
From Proteopedia
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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 Wed Nov 21 03:17:15 2007
