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Literature summary for 2.7.8.B13 extracted from

  • Grave, K.; Bennett, M.D.; Hoegbom, M.
    Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis (2019), Commun. Biol., 2, 175 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.B13

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of PgsA1 in absence of substrates (2.9 A), in complex with Mn2+ and citrate (1.9 A), and with the CDP-DAG substrate (1.8 A). The nucleotide moiety of the substrate is bound into a cleft formed by transmembrane helices 1-3, lined by G72, A75, and G85 and exposed to solvent. The long acyl chains of the substrate are disordered Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
A90Y about 25% of wild-type activity Mycobacterium tuberculosis
R137K about 115% of wild-type activity Mycobacterium tuberculosis
R137Q about 40% of wild-type activity Mycobacterium tuberculosis
R94K about 20% of wild-type activity Mycobacterium tuberculosis
R94Q about 15% of wild-type activity Mycobacterium tuberculosis
Y133E about 15% of wild-type activity Mycobacterium tuberculosis
Y133F about 125% of wild-type activity Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ both Mg2+ and Mn2+ support catalysis. A di-nuclear metal binding site is coordinated by residues D68, D71, D89, and D93 of the conserved sequence motif Mycobacterium tuberculosis
Mn2+ both Mg2+ and Mn2+ support catalysis. A di-nuclear metal binding site is coordinated by residues D68, D71, D89, and D93 of the conserved sequence motif Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPG7
-
-
Mycobacterium tuberculosis H37Rv P9WPG7
-
-

Subunits

Subunits Comment Organism
dimer crystallization data Mycobacterium tuberculosis