TAILIEUCHUNG - Báo cáo khoa học: Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92

Starting with oligopeptide sequences and using PCR, the gene of the cyclodextrinase fromFlavobacteriumsp. no. 92 wasderivedfrom sequenced and expressed inEscherichia coli; the gene pro-duct was purified and crystallized. An X-ray diffraction analysis using seleno-methionines with multiwavelength anomalous diffraction techniques yielded the refined 3D structure at A ˚ resolution. | Eur. J. Biochem. 270 2332-2341 2003 FEBS 2003 doi Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92 Hanna B. Fritzsche Torsten Schwede and Georg E. Schulz Institut fur Organische Chemie und Biochemie Albert-Ludwigs-Universiteit Freiburg im Breisgau Germany Starting with oligopeptide sequences and using PCR the gene of the cyclodextrinase from Flavobacterium sp. no. 92 was derived from the genomic DNA. The gene wws sequenced and expressed in Escherichia coli the gene product was purified and crystallized. An X-ray diffraction analysis using seleno-methionines with multiwavelength anomalous diffraction techniques yielded the refined 3D structure at A resolution. hhe enzyme hydrolyzes a 1 4 -glycosidic bonds of cyclodextrins and linear malto-oligosaccharides. It belongs to the glycosylhydrolase family no. 13 and has a chain fold similar to that of a-amylases cyclodextrin glycosyltransferases and other cyclodextrinases. In contrast with most family members but in agreement with other cyclodextrinases the enzyme contains an additional characteristic N-terminal domain of about 100 residues. This domain participates in the formation of a putative D2-sym-metric tetramer but not in cyclodextrin binding at the active center as observed with the other cyclodextrinases. Moreover the domain is located at a position quite different from that of the other cyclodextrinases. Whether oligomerization facilitates the cyclodextrin deformation required for hydrolysis is discussed. Keywords calcium-binding site cyclodextrin degradation glycosylhydrolase family no. 13 oligomerization X-ray analysis. Cyclodextrins CDs are cyclic malto-oligosaccharides of at least six to generally eight glucosyl units linked via a 1 4 -glycosidic bonds. hheir ability to form inclusion complexes with numerous small hydrophobic molecules is used in various applications such as microencapsulation of drugs 1 and chromatographic .

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