Structure of Acidothermus cellulolyticus Family 74 Glycoside Hydrolase at 1.82 Angstrom Resolution: Article No. F69

Petri Alahuhta, Vladimir Lunin, Michael Himmel, William Adney

Research output: Contribution to journalArticlepeer-review

Abstract

Here, a 1.82 A 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.
Original languageAmerican English
Pages (from-to)1335-1338
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume69
Issue number12
DOIs
StatePublished - 2013

NREL Publication Number

  • NREL/JA-2700-60609

Keywords

  • endoglucanases
  • GH74
  • glycoside hydrolases
  • xyloglucanases

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