1TIA

AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES

Summary for 1TIA

• Entry DOI: 10.2210/pdb1tia/pdb
• Descriptor: LIPASE (1 entity in total)
• Functional Keywords: hydrolase(carboxylic esterase)
• Biological source: Penicillium camemberti
• Total number of polymer chains: 1
• Total formula weight: 30205.53

Authors

Derewenda, U.,Swenson, L.,Yamaguchi, S.,Wei, Y.,Derewenda, Z.S. (deposition date: 1993-12-06, release date: 1995-01-26, Last modification date: 2024-02-14)

Primary citation

Derewenda, U.,Swenson, L.,Green, R.,Wei, Y.,Dodson, G.G.,Yamaguchi, S.,Haas, M.J.,Derewenda, Z.S.
An unusual buried polar cluster in a family of fungal lipases.
Nat.Struct.Biol., 1:36-47, 1994

PubMed Abstract: 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.

PubMed: 7656005
DOI: 10.1038/nsb0194-36

Experimental method

X-RAY DIFFRACTION (2.1 Å)