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Structure paper

TitleImportance of Arg-599 of b-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop
Journal, issue, pagesBiochem. Cell Biol., Vol. 88, Page 969-979, Year 2010
Publish dateMay 3, 2010 (structure data deposition date)
AuthorsDugdale, M.L. / Vance, M.L. / Wheatley, R.W. / Driedger, M.R. / Nibber, A. / Tran, A. / Huber, R.E.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-3muz:
E.Coli (lacZ) beta-galactosidase (R599A) in complex with IPTG
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3mv0:
E. COLI (lacZ) BETA-GALACTOSIDASE (R599A) IN COMPLEX WITH D-GALCTOPYRANOSYL-1-ONE
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3mv1:
E.Coli (lacZ) beta-galactosidase (R599A) in complex with Guanidinium
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-IPT:
1-methylethyl 1-thio-beta-D-galactopyranoside

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

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

ChemComp-HOH:
WATER

ChemComp-149:
D-galactonolactone

ChemComp-GAI:
GUANIDINE

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Arg-599-Ala / BETA-GALACTOSIDASE / HYDROLASE TIM BARREL(ALPHA/BETA BARREL) / JELLY-ROLL BARREL / IMMUNOGLOBULIN BETA SUPERSANDWHICH / GLYCOSIDASE

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