2QCX

Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine

Summary for 2QCX

• Entry DOI: 10.2210/pdb2qcx/pdb
• Descriptor: Transcriptional activator tenA, N-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-N-(2-HYDROXYETHYL)FORMAMIDE (3 entities in total)
• Functional Keywords: up-down bundle, hydrolase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 61528.46

Authors

Zhang, Y.,Jenkins, A.L.,Begley, T.P.,Ealick, S.E. (deposition date: 2007-06-19, release date: 2007-10-23, Last modification date: 2023-08-30)

Primary citation

Jenkins, A.L.,Zhang, Y.,Ealick, S.E.,Begley, T.P.
Mutagenesis studies on TenA: A thiamin salvage enzyme from Bacillus subtilis
Bioorg.Chem., 36:29-32, 2008

PubMed Abstract: TenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described.

PubMed: 18054064
DOI: 10.1016/j.bioorg.2007.10.005

Experimental method

X-RAY DIFFRACTION (2.2 Å)