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TitleDimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
Journal, issue, pagesJ. Mol. Biol., Vol. 356, Page 57-71, Year 2006
Publish dateJul 13, 2005 (structure data deposition date)
AuthorsCrennell, S.J. / Cook, D. / Minns, A. / Svergun, D. / Andersen, R.L. / Nordberg Karlsson, E.
External linksJ. Mol. Biol. / PubMed:16343530
MethodsX-ray diffraction
Resolution1.54 - 2.15 Å
Structure data

PDB-2bw8:
Native structure of Endoglucanase 12A (Cel12A) from Rhodothermus marinus
Method: X-RAY DIFFRACTION / Resolution: 1.54 Å

PDB-2bwa:
Structure of Endoglucanase 12A (Cel12A) from Rhodothermus marinus in complex with cellopentaose, 20 minute soak.
Method: X-RAY DIFFRACTION / Resolution: 1.68 Å

PDB-2bwc:
Structure of Endoglucanase 12A (Cel12A) from Rhodothermus marinus in complex with cellopentaose (5 minute soak)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-GLC:
alpha-D-glucopyranose

Source
  • rhodothermus marinus (bacteria)
KeywordsHYDROLASE / ENDOGLUCANASE / CELLULASE / GLYCOSIDE HYDROLASE FAMILY 12 / CELLOPENTAOSE

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