1R9G

Three-dimensional Structure of YaaE from Bacillus subtilis

Summary for 1R9G

• Entry DOI: 10.2210/pdb1r9g/pdb
• Descriptor: Hypothetical protein yaaE (2 entities in total)
• Functional Keywords: triad amidotransferase, glutaminase, alpha/beta protein, cofactor biosynthesis, transferase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 47846.70

Authors

Bauer, J.A.,Bennett, E.M.,Begley, T.P.,Ealick, S.E. (deposition date: 2003-10-29, release date: 2004-01-27, Last modification date: 2024-10-30)

Primary citation

Bauer, J.A.,Bennett, E.M.,Begley, T.P.,Ealick, S.E.
Three-dimensional Structure of YaaE from Bacillus subtilis, a Glutaminase Implicated in Pyridoxal-5'-phosphate Biosynthesis.
J.Biol.Chem., 279:2704-2711, 2004

PubMed Abstract: The structure of YaaE from Bacillus subtilis was determined at 2.5-A resolution. YaaE is a member of the triad glutamine aminotransferase family and functions in a recently identified alternate pathway for the biosynthesis of vitamin B(6). Proposed active residues include conserved Cys-79, His-170, and Glu-172. YaaE shows similarity to HisH, a glutaminase involved in histidine biosynthesis. YaaD associates with YaaE. A homology model of this protein was constructed. YaaD is predicted to be a (beta/alpha)(8) barrel on the basis of sequence comparisons. The predicted active site includes highly conserved residues 211-216 and 233-235. Finally, a homology model of a putative YaaD-YaaE complex was prepared using the structure of HisH-F as a model. This model predicts that the ammonia molecule generated by YaaE is channeled through the center of the YaaD barrel to the putative YaaD active site.

PubMed: 14585832
DOI: 10.1074/jbc.M310311200

Experimental method

X-RAY DIFFRACTION (2.5 Å)