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TitleStructures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.
Journal, issue, pagesJ. Mol. Biol., Vol. 300, Page 611-617, Year 2000
Publish dateMar 14, 2000 (structure data deposition date)
AuthorsPrag, G. / Papanikolau, Y. / Tavlas, G. / Vorgias, C.E. / Petratos, K. / Oppenheim, A.B.
External linksJ. Mol. Biol. / PubMed:10884356
MethodsX-ray diffraction
Resolution1.8 - 1.9 Å
Structure data

PDB-1c7s:
BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1c7t:
BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • serratia marcescens (bacteria)
KeywordsHYDROLASE / GLYCOSYL HYDROLASE / BETA-N-ACETYLHEXOSAMINIDASE / CHITINOLYSIS / A/B(TIM)-BARREL / SITE DIRECTED MUTAGENESIS / SUBSTRATE NUCLEOPHILE STABILIZER MUTATION / CHITINOLYSIN / PROTON DONOR / CO-CRYSTAL STRUCTURE

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