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TitleAspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state.
Journal, issue, pagesJ. Biol. Chem., Vol. 277, Page 40055-40065, Year 2002
Publish dateJun 11, 2002 (structure data deposition date)
AuthorsWilliams, S.J. / Mark, B.L. / Vocadlo, D.J. / James, M.N. / Withers, S.G.
External linksJ. Biol. Chem. / PubMed:12171933
MethodsX-ray diffraction
Resolution1.9 - 2.1 Å
Structure data

PDB-1m01:
Wildtype Streptomyces plicatus beta-hexosaminidase in complex with product (GlcNAc)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1m03:
Mutant Streptomyces plicatus beta-hexosaminidase (D313A) in complex with product (GlcNAc)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1m04:
Mutant Streptomyces plicatus beta-hexosaminidase (D313N) in complex with product (GlcNAc)
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • streptomyces plicatus (bacteria)
KeywordsHYDROLASE / substrate assisted catalysis / streptomyces plicatus / hexosaminidase / TIM barrel / family 20 glycosidase / beta-hexosaminidase

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