1zfn
From Proteopedia
Structural Analysis of Escherichia coli ThiF
Overview
Escherichia coli ThiF is an enzyme in the biosynthetic cascade for generating the essential cofactor thiamin pyrophosphate. In this cascade, ThiF catalyzes adenylation of the C terminus of ThiS. We report here the crystal structures of ThiF, alone and in complex with ATP. The structures provide insight into a preference for ATP during adenylation of the protein ThiS. Additionally, the structures reveal an ordered crossover loop predicted to clamp the flexible tail of ThiS into the ThiF active site during the adenylation reaction. The importance of the crossover loop for ThiF activity is highlighted by mutational analysis. Comparison of ThiF with the structural homologues MoeB, APPBP1-UBA3, and SAE1-SAE2 reveals that the ATP-binding site, including an arginine-finger, is maintained throughout evolution, and shows divergence occurring in protein substrate-binding sites and regions devoted to unique steps in the specific function of each enzyme.
About this Structure
1ZFN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural analysis of Escherichia coli ThiF., Duda DM, Walden H, Sfondouris J, Schulman BA, J Mol Biol. 2005 Jun 17;349(4):774-86. PMID:15896804 Page seeded by OCA on Sat May 3 17:34:03 2008
Categories: Escherichia coli | Single protein | Duda, D M. | Schulman, B A. | Sfondouris, J. | Walden, H. | Adenylation | Atp-binding | P-loop | Rossman fold | Thif | These
