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TitleReversing the roles of a crucial hydrogen-bonding pair: a lysine-insensitive mutant of Campylobacter jejuni dihydrodipicolinate synthase, H59K, binds histidine in its allosteric site
Journal, issue, pagesTo Be Published
Publish dateOct 11, 2020 (structure data deposition date)
AuthorsYazdi, M.M. / Saran, S. / Sanders, D.A.R. / Palmer, D.R.J.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.89 - 2.28 Å
Structure data

PDB-7kel:
Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in the active site
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-7kg2:
Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in the active site and L-histidine bound at the allosteric site
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-7kxg:
Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and L-histidine bound at the allosteric site
Method: X-RAY DIFFRACTION / Resolution: 2.28 Å

PDB-7lbd:
Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in the active site in C2221 space group
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-ACT:
ACETATE ION

ChemComp-MG:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-HIS:
HISTIDINE

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

Source
  • campylobacter jejuni (Campylobacter)
  • campylobacter jejuni subsp. jejuni serotype o:2 (strain atcc 700819 / nctc 11168) (Campylobacter)
KeywordsLYASE / DIHYDRODIPICOLINATE SYNTHASE

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