A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family
Tekijät: Sinha S, Rappu P, Lange SC, Mantsala P, Zalkin H, Smith JL
Kustantaja: NATL ACAD SCIENCES
Julkaisuvuosi: 1999
Lehti:: Proceedings of the National Academy of Sciences of the United States of America
Tietokannassa oleva lehden nimi: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Lehden akronyymi: P NATL ACAD SCI USA
Vuosikerta: 96
Numero: 23
Aloitussivu: 13074
Lopetussivu: 13079
Sivujen määrä: 6
ISSN: 0027-8424
DOI: https://doi.org/10.1073/pnas.96.23.13074
Tiivistelmä
The yabJ gene in Bacillus subtilis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein, The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7-Angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity, The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.
The yabJ gene in Bacillus subtilis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein, The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7-Angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity, The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.
Turun yliopiston Tutkimustietojärjestelmän portaali