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Structure paper

TitleAllomorphy as a mechanism of post-translational control of enzyme activity.
Journal, issue, pagesNat Commun, Vol. 11, Page 5538-5538, Year 2020
Publish dateMar 20, 2020 (structure data deposition date)
AuthorsWood, H.P. / Cruz-Navarrete, F.A. / Baxter, N.J. / Trevitt, C.R. / Robertson, A.J. / Dix, S.R. / Hounslow, A.M. / Cliff, M.J. / Waltho, J.P.
External linksNat Commun / PubMed:33139716
MethodsX-ray diffraction
Resolution1.04 - 2.1 Å
Structure data

PDB-6ydj:
P146A variant of beta-phosphoglucomutase from Lactococcus lactis in complex with glucose 6-phosphate and trifluoromagnesate
Method: X-RAY DIFFRACTION / Resolution: 1.04 Å

PDB-6ydk:
Substrate-free P146A variant of beta-phosphoglucomutase from Lactococcus lactis
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-6ydl:
Substrate-free beta-phosphoglucomutase from Lactococcus lactis
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-6ydm:
beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-BG6:
6-O-phosphono-beta-D-glucopyranose

ChemComp-MGF:
TRIFLUOROMAGNESATE

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PDO:
1,3-PROPANDIOL

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

ChemComp-ACT:
ACETATE ION

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • lactococcus lactis subsp. lactis (strain il1403) (lactic acid bacteria)
KeywordsISOMERASE / transition-state analogue / cis-trans proline isomerization / allomorphy / phosphoryl transfer / enzyme regulation / citrate

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