Document Detail


1.8 A refined structure of the lipase from Geotrichum candidum.
MedLine Citation:
PMID:  8464065     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A lipase from the fungus Geotrichum candidum is one of only three interfacially activated lipases whose structures have been reported to date. We have previously reported the partially refined 2.2 A structure of this enzyme. We have subsequently extended the resolution and here report the fully refined 1.8 A structure of this lipase. The structure observed in the crystal is apparently not the lipolytic conformation, as the active site is not accessible from the surface of the molecule. A single large cavity is found in the interior of the molecule and extends from the catalytic Ser to two surface helices, suggesting that this face may be the region that interacts with the lipid interface. The mobility of local segments on this face is indicated by temperature factors larger than elsewhere in the molecule and by the observation of several residues whose side-chains are discretely disordered. These observations strongly suggest that this portion of the molecule is involved in interfacial and substrate binding, but the exact nature of the conformational changes induced by binding to the lipid interface can not be determined.
Authors:
J D Schrag; M Cygler
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular biology     Volume:  230     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1993 Mar 
Date Detail:
Created Date:  1993-04-30     Completed Date:  1993-04-30     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  575-91     Citation Subset:  IM    
Affiliation:
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Disulfides / analysis
Geotrichum / enzymology*
Glycosylation
Lipase / chemistry*
Models, Molecular
Models, Structural
Protein Structure, Secondary*
Software
Thermodynamics
X-Ray Diffraction / methods
Chemical
Reg. No./Substance:
0/Disulfides; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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