Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate
| Autor: | Guy Vandenbussche, Jean Marie Ruysschaert, Patrick Van Gelder, Kris Pauwels, Remy Loris, Lode Wyns |
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| Rok vydání: | 2005 |
| Předmět: |
Burkholderia
Biophysics Biochemistry law.invention Crystal Bacterial Proteins X-Ray Diffraction Structural Biology law Genetics Burkholderia glumae Lipase Crystallization biology Chemistry Space group Periplasmic space Condensed Matter Physics biology.organism_classification Crystallography Crystallization Communications X-ray crystallography Foldase biology.protein Electrophoresis Polyacrylamide Gel Molecular Chaperones |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:791-795 |
| ISSN: | 1744-3091 |
| Popis: | Bacterial lipases that are secreted via the type II secretion pathway require a lipase-specific foldase in order to obtain their native and biologically active conformation in the periplasmic space. The lipase-foldase complex from Burkholderia glumae (319 and 333 residues, respectively) was crystallized in two crystal forms. One crystal form belongs to space group P3(1)21 (P3(2)21), with unit-cell parameters a = b = 122.3, c = 98.2 A. A procedure is presented which improved the diffraction of these crystals from approximately 5 to 2.95 A. For the second crystal form, which belonged to space group C2 with unit-cell parameters a = 183.0, b = 75.7, c = 116.6 A, X-ray data were collected to 1.85 A. |
| Databáze: | OpenAIRE |
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