Mycobacterium tuberculosis Pantothenate kinase mutant F247A/F254A

Biochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region of Mycobacterium tuberculosis pantothenate kinase

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis.

Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK.

Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action.

M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations.

Location and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action.

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.

2% PEG 400,
2.0 M Ammonium sulphate,
100mM HEPES sodium salt

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Homodimer, CoA biosynthesis, Nucleotide binding, Concerted movement, Structural transformation, TRANSFERASE