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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The accessory domain changes the accessibility and molecular topography of the catalytic interface in monomeric GH39 ss-xylosidases

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Author(s):
Santos, Camila Ramos [1] ; Polo, Carla Cristina [1] ; Correa, Juliana Moco [2] ; Garcia Simao, Rita de Cassia [2] ; Vicente Seixas, Flavio Augusto [3] ; Murakami, Mario Tyago [1]
Total Authors: 6
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Oeste Parana, Ctr Ciencias Med & Farmaceut, BR-85814110 Cascavel, Pr - Brazil
[3] Univ Estadual Maringa, Dept Bioquim, BR-87020900 Maringa, Parana - Brazil
Total Affiliations: 3
Document type: Journal article
Source: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY; v. 68, n. 10, p. 1339-1345, OCT 2012.
Web of Science Citations: 11
Abstract

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. (AU)

FAPESP's process: 10/51890-8 - SMOLBnet 2.0: Structural studies of transcription factors involved in the regulation of hydrolytic enzyme genes and swollenin from Aspergillus niger and A. fumigatus
Grantee:Mário Tyago Murakami
Support type: Regular Research Grants