1ZFN

Structural Analysis of Escherichia coli ThiF

Summary for 1ZFN

• Entry DOI: 10.2210/pdb1zfn/pdb
• Related: 1JW9 1JWA 1JWB
• Descriptor: Adenylyltransferase thiF, ZINC ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: rossmann fold, p-loop, atp-binding, adenylation, this, thif, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 110833.70

Authors

Duda, D.M.,Walden, H.,Sfondouris, J.,Schulman, B.A. (deposition date: 2005-04-20, release date: 2005-06-14, Last modification date: 2024-02-14)

Primary citation

Duda, D.M.,Walden, H.,Sfondouris, J.,Schulman, B.A.
Structural Analysis of Escherichia Coli ThiF.
J.Mol.Biol., 349:774-786, 2005

PubMed Abstract: 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.

PubMed: 15896804
DOI: 10.1016/j.jmb.2005.04.011

Experimental method

X-RAY DIFFRACTION (2.75 Å)