Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis. Academic Article

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.

authors

• Begley, Tadhg

published proceedings

• J Biol Chem

altmetric score

• 3

author list (cited authors)

• Bauer, J. A., Bennett, E. M., Begley, T. P., & Ealick, S. E.

citation count

• 43

complete list of authors

• Bauer, Jacob A||Bennett, Eric M||Begley, Tadhg P||Ealick, Steven E

publication date

• January 2004

publisher

• Elsevier  Publisher

keywords

• Amino Acid Sequence
• Bacillus Subtilis
• Bacterial Proteins
• Binding Sites
• Glutaminase
• Models, Molecular
• Molecular Sequence Data
• Protein Binding
• Protein Conformation
• Pyridoxal Phosphate
• Structure-Activity Relationship

Digital Object Identifier (DOI)

• 10.1074/jbc.M310311200

start page

• 2704

end page

• 2711

volume

• 279

issue

• 4

URL

• http%3A%2F%2Fdx.doi.org%2F10.1074%2Fjbc.m310311200