SABIN, Charles, Michaela WIMMEROVÁ, Martina BUDOVÁ, Lenka ŠNAJDROVÁ, Catherine GAUTIER, Jaroslav KOČA, Edward MITCHELL, Nechama GILBOA-GARBER and Anne IMBERTY. Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides. Online. In 12th European Carbohydrate Symposium. Grenoble, France: CERMAV-CNRS, 2003. p. 390. [citováno 2024-04-23]
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Basic information
Original name Structural and thermodynamical characterisation of interaction between a pseudomonas lectin and monosaccharides
Authors SABIN, Charles (250 France), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Martina BUDOVÁ (250 France), Lenka ŠNAJDROVÁ (250 France), Catherine GAUTIER (250 France), Jaroslav KOČA (376 Israel), Edward MITCHELL (250 France), Nechama GILBOA-GARBER (376 Israel) and Anne IMBERTY (250 France)
Edition Grenoble, France, 12th European Carbohydrate Symposium, p. 390-390, 2003.
Publisher CERMAV-CNRS
Other information
Original language English
Type of outcome Proceedings paper
Field of Study 10600 1.6 Biological sciences
Country of publisher France
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/03:00008865
Organization unit Faculty of Science
Keywords in English Pseudomonas aeruginosa; lectin; microcalorimetry; crystal structure; cystic fibrosis
Tags Crystal Structure, cystic fibrosis, lectin, microcalorimetry, Pseudomonas aeruginosa
Tags International impact
Changed by Changed by: prof. RNDr. Michaela Wimmerová, Ph.D., učo 854. Changed: 15/11/2006 11:39.
Abstract
Pseudomonas aeruginosa galactose- and fucose-binding (PA-IL and PA-IIL) lectins contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL complexed with fucose has been solved at 1.3 A and further refined at 1 Ĺ resolution. Additional experiments have been performed in order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Crystals have been obtained for the complex between PA-ILL and b-Me-D-arabinopyranoside and the structure has been solved at 1.8 A resolution. PA-IIL exhibits unusually high specificity to fucose, which can be related to the presence of two calcium ions in the site. Isothermal titration microcalorimetry (ITC) experiments were performed in order to characterize the thermodynamic parameters of the interaction since this method has been proven to be well adapted to the study of protein/carbohydrate interactions. Several monosaccharides differing only by the group at C5 (L-fucose, L-galactose and D-arabinose) were tested, as well as their methyl-glycosides. Calculations of charges distribution were performed using quantum chemistry in order to rationalize the role of calcium ions in the affinity.
Links
LN00A016, research and development projectName: BIOMOLEKULÁRNÍ CENTRUM
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center
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