4LGN
The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase
Summary for 4LGN
| Entry DOI | 10.2210/pdb4lgn/pdb |
| Descriptor | Cellulose-binding, family II, POTASSIUM ION, 1,2-ETHANEDIOL, ... (8 entities in total) |
| Functional Keywords | gh74, xyloglucanase, cellulose binding protein |
| Biological source | Acidothermus cellulolyticus |
| Total number of polymer chains | 1 |
| Total formula weight | 81456.34 |
| Authors | Alahuhta, P.M.,Lunin, V.V. (deposition date: 2013-06-28, release date: 2013-12-11, Last modification date: 2023-09-20) |
| Primary citation | Alahuhta, M.,Adney, W.S.,Himmel, M.E.,Lunin, V.V. Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 angstrom resolution. Acta Crystallogr.,Sect.F, 69:1335-1338, 2013 Cited by PubMed 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. PubMed: 24316824DOI: 10.1107/S1744309113030005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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