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TitleBiochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region of Mycobacterium tuberculosis pantothenate kinase
Journal, issue, pagesActa Crystallogr F Struct Biol Commun, Vol. 73, Page 635-643, Year 2017
Publish dateMay 11, 2017 (structure data deposition date)
AuthorsPaul, A. / Kumar, P. / Surolia, A. / Vijayan, M.
External linksActa Crystallogr F Struct Biol Commun / PubMed:29095158
MethodsX-ray diffraction
Resolution1.8 - 3.2 Å
Structure data

PDB-5xlv:
Mycobacterium tuberculosis Pantothenate kinase mutant F254A
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5xlw:
Mycobacterium tuberculosis Pantothenate kinase mutant F247A/F254A
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-5xmb:
Mycobacterium tuberculosis Pantothenate kinase mutant F247A
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsTRANSFERASE / Homodimer / CoA biosynthesis / Nucleotide binding / Concerted movement / Structural transformation

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