1QD9

Bacillus subtilis YABJ

Summary for 1QD9

• Entry DOI: 10.2210/pdb1qd9/pdb
• Descriptor: PURINE REGULATORY PROTEIN YABJ, MERCURY (II) ION, ACETIC ACID, ... (5 entities in total)
• Functional Keywords: perchloric acid soluble protein, purine regulation, yjgf/yer057c family, gene regulation
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: P37552
• Total number of polymer chains: 3
• Total formula weight: 41629.32

Authors

Smith, J.L.,Sinha, S.,Rappu, P.,Lange, S.C.,Mantsala, P.,Zalkin, H. (deposition date: 1999-07-09, release date: 1999-11-26, Last modification date: 2024-02-14)

Primary citation

Sinha, S.,Rappu, P.,Lange, S.C.,Mantsala, P.,Zalkin, H.,Smith, J.L.
Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family.
Proc.Natl.Acad.Sci.USA, 96:13074-13079, 1999

PubMed Abstract: 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-A 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.

PubMed: 10557275
DOI: 10.1073/pnas.96.23.13074

Experimental method

X-RAY DIFFRACTION (1.7 Å)