Open AccessStructure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 Å resolution
Author(s) -
Alahuhta Markus,
Adney William S.,
Himmel Michael E.,
Lunin Vladimir V.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113030005
Subject(s) - clostridium thermocellum , glycoside hydrolase , hydrolase , chemistry , active site , enzyme , resolution (logic) , stereochemistry , derivative (finance) , biochemistry , cellulase , computer science , financial economics , artificial intelligence , economics
Here, a 1.82 Å resolution X‐ray structure of a glycoside hydrolase family 74 (GH74) enzyme from Acidothermus cellulolyticus is reported. The resulting structure was refined to an R factor of 0.150 and an R free of 0.196. Structural analysis shows that five related structures have been reported with a secondary‐structure similarity of between 75 and 89%. The five similar structures were all either Clostridium thermocellum or Geotrichum sp. M128 GH74 xyloglucanases. Structural analysis indicates that the A. cellulolyticus GH74 enzyme is an endoxyloglucanase, as it lacks a characteristic loop that blocks one end of the active site in exoxyloglucanases. Superimposition with the C. thermocellum GH74 shows that Asp451 and Asp38 are the catalytic residues.