Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family
AUTOR(ES)
Sinha, Sangita
FONTE
The National Academy of Sciences
RESUMO
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-Å 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23902Documentos Relacionados
- Complex Metabolic Phenotypes Caused by a Mutation in yjgF, Encoding a Member of the Highly Conserved YER057c/YjgF Family of Proteins
- A Role for a Highly Conserved Protein of Unknown Function in Regulation of Bacillus subtilis purA by the Purine Repressor
- Reduced Transaminase B (IlvE) Activity Caused by the Lack of yjgF Is Dependent on the Status of Threonine Deaminase (IlvA) in Salmonella enterica Serovar Typhimurium
- Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP
- Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16