Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE OPEN CONFORMATION OF A PSEUDOMONAS LIPASE
Autore:
SCHRAG JD; LI YG; CYGLER M; LANG DM; BURGDORF T; HECHT HJ; SCHMID R; SCHOMBURG D; RYDEL TJ; OLIVER JD; STRICKLAND LC; DUNAWAY CM; LARSON SB; DAY J; MCPHERSON A;
Indirizzi:
NATL RES COUNCIL CANADA,BIOTECHNOL RES INST,6100 ROYALMOUNT AVE MONTREAL PQ H4P 2R2 CANADA GBF,DEPT MOL STRUCT RES D-38124 BRAUNSCHWEIG GERMANY UNIV STUTTGART,INST TECH BIOCHEM D-70569 STUTTGART GERMANY PROCTER & GAMBLE CO,MIAMI VALLEY LABS CINCINNATI OH 45253 UNIV CALIF RIVERSIDE,DEPT BIOCHEM RIVERSIDE CA 92521
Titolo Testata:
Structure
fascicolo: 2, volume: 5, anno: 1997,
pagine: 187 - 202
SICI:
0969-2126(1997)5:2<187:TOCOAP>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANDIDA-RUGOSA LIPASE; INTERFACIAL ACTIVATION; TRIACYLGLYCEROL LIPASE; PANCREATIC LIPASE; CRYSTAL-STRUCTURE; TRIAD FORMS; REFINEMENT; COMPLEX; CEPACIA; CLONING;
Keywords:
CRYSTALLOGRAPHY; ALPHA/BETA-HYDROLASE FOLD; INTERFACIAL ACTIVATION; LIPASE; 3-DIMENSIONAL STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
J.D. Schrag et al., "THE OPEN CONFORMATION OF A PSEUDOMONAS LIPASE", Structure, 5(2), 1997, pp. 187-202

Abstract

Background: The interfacial activation of lipases results primarily from conformational changes in the enzymes which expose the active siteand provide a hydrophobic surface for interaction with the lipid substrate, Comparison of the crystallization conditions used and the structures observed for a variety of lipases suggests that the enzyme conformation is dependent on solution conditions. Pseudomonas cepacia lipase (PCL) was crystallized in conditions from which the open, active conformation of the enzyme was expected. Its three-dimensional structure was determined independently in three different laboratories and was compared with the previously reported closed conformations of the closely related lipases from Pseudomonas glumae (PGL) and Chromobacterium viscosum (CVL). These structures provide new insights into the functionof this commercially important family of lipases. Results: The three independent structures of PCL superimpose with only small differences in the mainchain conformations, As expected, the observed conformationreveals a catalytic site exposed to the solvent, Superposition of PCLwith the PGL and CVL structures indicates that the rearrangement fromthe closed to the open conformation involves three loops. The largestmovement involves a 40 residue stretch, within which a helical segment moves to afford access to the catalytic site. A hydrophobic cleft that is presumed to be the lipid-binding site is formed around the active site, Conclusions: The interfacial activation of Pseudomonas lipasesinvolves conformational rearrangements of surface loops and appears to conform to models of activation deduced from the structures of fungal and mammalian lipases. Factors controlling the conformational rearrangement are not understood, but a comparison of crystallization conditions and observed conformation suggests that the conformation of the protein is determined by the solution conditions, perhaps by the dielectric constant.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 19:58:04