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Structure paper

TitleBeneficial mutations occurring in E. coli pyruvate kinase afford new allosteric mechanisms leading to faster resumption of growth
Journal, issue, pagesTo Be Published
Publish dateSep 5, 2022 (structure data deposition date)
AuthorsDonovan, K.A. / Coombes, D. / Dobson, R.C.J. / Cooper, T.F.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.01 - 2.88 Å
Structure data

PDB-8edq:
E. coli pyruvate kinase (PykF) I264F
Method: X-RAY DIFFRACTION / Resolution: 2.88 Å

PDB-8edr:
E. coli pyruvate kinase (PykF) P70Q
Method: X-RAY DIFFRACTION / Resolution: 2.64 Å

PDB-8eds:
Escherichia coli pyruvate kinase (PykF) P70Q
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-8edt:
E. coli Pyruvate kinase (PykF) T462I
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-8eq0:
Escherichia coli pyruvate kinase G381A
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

PDB-8eq1:
Escherichia coli pyruvate kinase D127N
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

PDB-8eq3:
Escherichia coli pyruvate kinase A301T
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-8eu4:
Escherichia coli pyruvate kinase A301S
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-B3P:
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

ChemComp-MLI:
MALONATE ION

ChemComp-IMD:
IMIDAZOLE

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Pyruvate kinase / Long term evolution experiment / Kinase

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