Insights into interfacial activation from an open structure of Candida rugosa lipase.
The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site. Comparison with the crystal structure of the homologous lipase from Geotrichum candidum, in which the active site is covered by surface loops and is inaccessible from the solvent, shows that the largest structural differences occur in the vicinity of the active site. Three loops in this region differ significantly in conformation, and the interfacial activation of these lipases is likely to be associated with conformational rearrangements of these loops. The "open" structure provides a new image of the substrate binding region and active site access, which is different from that inferred from the structure of the "closed" form of the G. candidum lipase.
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
P
P
Grochulski
Y
Y
Li
J D
JD
Schrag
F
F
Bouthillier
P
P
Smith
D
D
Harrison
B
B
Rubin
M
M
Cygler
D000595:Amino Acid Sequence; D001665:Binding Sites; D002175:Candida / Q000201:enzymology*; D004789:Enzyme Activation; D005848:Geotrichum / Q000201:enzymology; D008049:Lipase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008958:Models, Molecular; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
D008049:Lipase