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1tia
From Proteopedia
Revision as of 21:39, 28 September 2014 by OCA (Talk | contribs)
1tia is a 1 chain structure with sequence from Penicillium camemberti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Derewenda U, Swenson L, Green R, Wei Y, Dodson GG, Yamaguchi S, Haas MJ, Derewenda ZS. An unusual buried polar cluster in a family of fungal lipases. Nat Struct Biol. 1994 Jan;1(1):36-47. PMID:7656005
