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Literature summary extracted from

  • Shenoy, A.R.; Capuder, M.; Draskovic, P.; Lamba, D.; Visweswariah, S.S.; Podobnik, M.
    Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis (2007), J. Mol. Biol., 365, 211-225.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.17 enzyme is a Fe3+-Mn2+-binuclear dimer, and the metal ions contribute to dimerization. Wild-type has a molecule of phosphate bound in the active site. Structure of mutants N97A lacking one of the Mn2+ coordinating residues and D66A that has a compromised cAMP hydrolytic activity Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.17 D66A compromised cAMP hydrolytic activity, crystallization data Mycobacterium tuberculosis
3.1.4.17 N97A almost complete loss of activity, lacks one of the Mn2+ coordinating residues Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.17 Fe3+
-
 Mycobacterium tuberculosis
3.1.4.17 Mn2+
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.17 Mycobacterium tuberculosis P9WP65 product of Rv0805 gene
-
3.1.4.17 Mycobacterium tuberculosis H37Rv P9WP65 product of Rv0805 gene
-

Subunits

EC Number Subunits Comment Organism
3.1.4.17 dimer crystallization data Mycobacterium tuberculosis