title: Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
abstract: During crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.
authors.affiliation: Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland.
authors.forename: Paweł
authors.initials: P
authors.lastname: Strzelczyk
authors.affiliation: Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland.
authors.forename: Grzegorz D
authors.initials: GD
authors.lastname: Bujacz
authors.affiliation: Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland.
authors.forename: Piotr
authors.initials: P
authors.lastname: Kiełbasiński
authors.affiliation: Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland.
authors.forename: Jarosław
authors.initials: J
authors.lastname: Błaszczyk
mesh_terms: D002175:Candida / Q000201:enzymology*; D018360:Crystallography, X-Ray; D006031:Glycosylation; D008049:Lipase / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D008049:Lipase