4ATW

The crystal structure of Arabinofuranosidase

Summary for 4ATW

• Entry DOI: 10.2210/pdb4atw/pdb
• Descriptor: ALPHA-L-ARABINOFURANOSIDASE DOMAIN PROTEIN (1 entity in total)
• Functional Keywords: hydrolase, taf, arabinofuranosidase, thermostable
• Biological source: THERMOTOGA MARITIMA MSB8
• Total number of polymer chains: 6
• Total formula weight: 330595.76

Authors

Dumbrepatil, A.,Song, H.-N.,Jung, T.-Y.,Kim, T.-J.,Woo, E.-J. (deposition date: 2012-05-10, release date: 2012-05-23, Last modification date: 2024-10-09)

Primary citation

Dumbrepatil, A.,Park, J.,Jung, T.-Y.,Song, H.-N.,Jang, M.,Han, N.S.,Kim, T.-J.,Woo, E.-J.
Structural Analysis of Alpha-L-Arabinofuranosidase from Thermotoga Maritima Reveals Characteristics for Thermostability and Substrate Specificity.
J.Microbiol.Biotech., 22:1724-, 2012

PubMed Abstract: An alpha-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.

PubMed: 23221536
DOI: 10.4014/JMB.1208.08043

Experimental method

X-RAY DIFFRACTION (3 Å)