Reference : Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp....
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/80430
Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38.
English
Wouters, J. [> > > >]
Georis, J. [> > > >]
Engher, D. [> > > >]
Vandenhaute, J. [> > > >]
Dusart, Jean [Université de Liège - ULg > Services administratifs généraux > R&D : Gestion opérationnelle >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Depiereux, E. [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
2001
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
57
Pt 12
1813-9
Yes (verified by ORBi)
International
0907-4449
Oxford
United Kingdom
[en] Amino Acid Sequence ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Endo-1,4-beta Xylanases ; Glutamic Acid/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Streptomyces/enzymology ; Xylosidases/chemistry
[en] Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177.
http://hdl.handle.net/2268/80430

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