| Literature DB >> 24316824 |
Markus Alahuhta1, William S Adney, Michael E Himmel, Vladimir V Lunin.
Abstract
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 Rfree 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.Entities:
Keywords: GH74; endoglucanases; glycoside hydrolases; xyloglucanases
Mesh:
Substances:
Year: 2013 PMID: 24316824 PMCID: PMC3855714 DOI: 10.1107/S1744309113030005
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091