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

Crystal structure of a putative exo-beta-1,3-galactanase from Bifidobacterium bifidum S17

Full text
Author(s):
Godoy, Andre S. [1] ; de Lima, Mariana Z. T. [1] ; Camilo, Cesar M. [2] ; Polikarpov, Igor [1]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Dept Fis Sao Carlos, Ave Trabalhador Saocarlense 400, BR-13560970 Sao Carlos, SP - Brazil
[2] Ctr Tecnol Canavieira, Fazenda Santo Antonio, POB 162, BR-13400970 Piracicaba, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 72, n. 4, p. 288-293, APR 2016.
Web of Science Citations: 1
Abstract

Given the current interest in second-generation biofuels, carbohydrate-active enzymes have become the most important tool to overcome the structural recalcitrance of the plant cell wall. While some glycoside hydrolase families have been exhaustively described, others remain poorly characterized, especially with regard to structural information. The family 43 glycoside hydrolases are a diverse group of inverting enzymes; the available structure information on these enzymes is mainly from xylosidases and arabinofuranosidase. Currently, only one structure of an exo-beta-1,3-galactanase is available. Here, the production, crystallization and structure determination of a putative exo-beta-1,3-galactanase from Bifidobacterium bifidum S17 (BbGal43A) are described. BbGal43A was successfully produced and showed activity towards synthetic galactosides. BbGal43A was subsequently crystallized and data were collected to 1.4 angstrom resolution. The structure shows a single-domain molecule, differing from known homologues, and crystal contact analysis predicts the formation of a dimer in solution. Further biochemical studies are necessary to elucidate the differences between BbGal43A and its characterized homologues. (AU)

FAPESP's process: 11/05712-3 - Structural and functional studies of beta-galactosidases from Xanthomonas campestris
Grantee:Andre Schutzer de Godoy
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 08/56255-9 - Structure and function of enzymes and auxiliary proteins from Trichoderma, active in cell-wall hydrolysis
Grantee:Igor Polikarpov
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO
Grantee:Igor Polikarpov
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 09/05328-9 - Expression, purification and cristalization studies of the ligand-binding domain of nuclear receptors PPAR-alpha e PPAR-gamma
Grantee:Andre Schutzer de Godoy
Support type: Scholarships in Brazil - Scientific Initiation