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TitleStudies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry
Journal, issue, pagesProtein J., Vol. 29, Page 26-31, Year 2010
Publish dateJul 14, 2009 (structure data deposition date)
AuthorsLo, S. / Dugdale, M.L. / Jeerh, N. / Ku, T. / Roth, N.J. / Huber, R.E.
External linksProtein J. / PubMed:19936901
MethodsX-ray diffraction
Resolution2 - 2.7 Å
Structure data

PDB-3iap:
E. coli (lacZ) beta-galactosidase (E416Q)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3iaq:
E. coli (lacz) beta-galactosidase (E416V)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-BTB:
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
KeywordsHYDROLASE / Glu-416-Gln BETA-GALACTOSIDASE HYDROLASE TIM BARREL(ALPHA/BETA BARREL) JELLY-ROLL BARREL IMMUNOGLOBULIN BETA SUPERSANDWHICH / Glycosidase / Glu-416-Val BETA-GALACTOSIDASE HYDROLASE TIM BARREL(ALPHA/BETA BARREL) JELLY-ROLL BARREL IMMUNOGLOBULIN BETA SUPERSANDWHICH

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