Structural Analysis of α-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity

Cited 11 time in scopus
Metadata Downloads
Title
Structural Analysis of α-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity
Author(s)
A Dumbrepatil; J M Park; Tae Yang Jung; Hyung Nam Song; M U Jang; N S Han; T J Kim; Eui-Jeon Woo
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 22, no. 12, pp. 1724-1730
Publication Year
2012
Abstract
An α-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the enzymatic characterization and structural analysis of TmAFase. Tight domain associations found in TmAFase, such as an inter-domain disulfide bond (Cys306 and Cys476) in each monomer, a novel extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) was identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates.
Keyword
α-l-arabinofuranosidaseStructural analysisThermotoga maritimaX-ray crystallography
ISSN
1017-7825
Publisher
South Korea
DOI
http://dx.doi.org/10.4014/jmb.1208.08043
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.