Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c

  title={Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c},
  author={S. Sinha and M. Wetterer and S. Sprang and J. Schultz and J. Linder},
  journal={The EMBO Journal},
  • S. Sinha, M. Wetterer, +2 authors J. Linder
  • Published 2005
  • Medicine, Biology
  • The EMBO Journal
  • Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N‐terminal α/β‐hydrolase domain and a C‐terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side‐activity. A canonical substrate‐defining lysine and a catalytic asparagine indispensable for mammalian adenylyl cyclase activity correspond to N342 and H402 in Rv1900c. Mutagenic analysis indicates that these residues are dispensable for activity of Rv1900c. Structures of the cyclase homology domain, solved… CONTINUE READING
    Autoinhibitory mechanism and activity-related structural changes in a mycobacterial adenylyl cyclase.
    • 2
    • Highly Influenced
    Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation
    • 23
    • PDF
    Crystal Structures of the Catalytic Domain of Human Soluble Guanylate Cyclase
    • 69


    Publications referenced by this paper.
    The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity
    • 103
    • PDF
    Adenylyl Cyclase Rv1264 from Mycobacterium tuberculosis Has an Autoinhibitory N-terminal Domain*
    • 56
    • PDF
    Structural analysis of adenylate cyclases from Trypanosoma brucei in their monomeric state
    • 57
    CyaG, a Novel Cyanobacterial Adenylyl Cyclase and a Possible Ancestor of Mammalian Guanylyl Cyclases*
    • 39
    • PDF
    Truncation and alanine-scanning mutants of type I adenylyl cyclase.
    • 116
    • Highly Influential
    A Guanylyl Cyclase from Paramecium with 22 Transmembrane Spans
    • 31
    • PDF