Premium
Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum
Author(s) -
Kozak Maciej
Publication year - 2006
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20531
Subject(s) - xylanase , radius of gyration , chemistry , small angle x ray scattering , trichoderma reesei , crystallography , molecule , monomer , gyration , scattering , hydrolysis , cellulase , polymer , organic chemistry , enzyme , geometry , physics , mathematics , optics
Xylanase ( endo ‐1,4‐β‐xylanase; EC 3.2.1.8) is an enzyme that catalyzes the hydrolysis reaction of xylan. The structure of the xylanase II (XYNII) molecule from Trichoderma longibrachoatum (formerly Trichoderma reesei ) in a solution and at different pH values has been studied by small‐ and wide‐angle scattering of synchrotron radiation (SAXS‐WAXS). Analysis of the radius of gyration that characterizes xylanase has confirmed the stability of the above enzyme structure (the radius of gyration varied from 1.65 to 1.74 nm). On the basis of the SAXS data, the low‐resolution structure of the xylanase molecule in solution has been reconstructed by using ab initio methods and programs DALAI_GA and DAMMIN. The full SAXS‐WAXS data set (0.15 > s > 9.5 nm −1 ) fed to the program GASBOR permitted us to construct a chain‐like spatial distribution of a dummy residues model of the xylanase molecule. The shape of the model molecules is similar to that of xylanase molecule in the crystal and shows the characteristic asymmetry that makes the molecule to resemble a right hand. © 2006 Wiley Periodicals, Inc. Biopolymers 83:95–102, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com