Journal
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume 68, Issue -, Pages 1339-1345Publisher
WILEY-BLACKWELL
DOI: 10.1107/S0907444912028491
Keywords
GH39 ss-xylosidases; Caulobacter crescentus; oligomerization
Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [10/51890-8]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [10/51890-8] Funding Source: FAPESP
Ask authors/readers for more resources
beta-Xylosidases (EC 3.2.1.37) are among the principal glycosyl hydrolases involved in the breakdown of hemicelluloses, catalyzing the reduction of xylooligosaccharides to free xylose. All GH39 beta-xylosidases structurally characterized to date display a modular multi-domain organization that assembles a tetrameric quaternary structure. In this work, the crystal structure and the SAXS molecular envelope of a new GH39 beta-xylosidase from Caulobacter crescentus (CcXynB2) have been determined. Interestingly, CcXynB2 is a monomer in solution and comparative structural analyses suggest that the shortened C-terminus prevents the formation of a stable tetramer. Moreover, CcXynB2 has a longer loop from the auxiliary domain (the long a-helix-containing loop) which makes a number of polar and hydrophobic contacts with the parental (a/beta)8-barrel domain, modifying the accessibility and the molecular topography of the catalytic interface. These interactions also maintain the accessory domain tightly linked to the catalytic core, which may be important for enzyme function and stability.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available