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TitleApparent Reversal of Allosteric Response in Mycobacterium tuberculosis MenD Reveals Links to Half-of-Sites Reactivity.
Journal, issue, pagesChembiochem, Vol. 26, Page e202400943-e202400943, Year 2025
Publish dateSep 24, 2024 (structure data deposition date)
AuthorsHo, N.A.T. / Given, F.M. / Stanborough, T. / Klein, M. / Allison, T.M. / Bulloch, E.M.M. / Jiao, W. / Johnston, J.M.
External linksChembiochem / PubMed:39945237
MethodsX-ray diffraction
Resolution2.3 - 2.42 Å
Structure data

PDB-9dqi:
D306N Mutant of M.tuberculosis MenD (SEPHCHC Synthase)
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

PDB-9dsn:
D306A Mutant of M.tuberculosis MenD (SEPHCHC Synthase)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-9dtv:
Structure of D141A mutant of M.tuberculosis MenD (SEPHCHC Synthase)
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-DNA:
1,4-dihydroxy-2-naphthoic acid

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FMT:
FORMIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / menaquinone biosynthesis / SEPHCHC Synthase / Mycobacterium tuberculosis / MenD mutant enzyme / allosteric regulator complex (DHNA) / mutant D306N / ThDP-dependent enzyme. / Mycobaterium tuberculosis / MenD / allosteric regulator / DHNA / cooperativity / allostery mutant / M.tuberculosis / allostery / MenD mutant D141A / SEPHCHC Synthase mutant

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