1IIN

thymidylyltransferase complexed with UDP-glucose

Summary for 1IIN

• Entry DOI: 10.2210/pdb1iin/pdb
• Related: 1IIM 1MP3 1MP4 1MP5
• Descriptor: glucose-1-phosphate thymidylyltransferase, URIDINE-5'-DIPHOSPHATE-GLUCOSE (3 entities in total)
• Functional Keywords: transferase
• Biological source: Salmonella enterica
• Total number of polymer chains: 4
• Total formula weight: 132206.01

Authors

Barton, W.A.,Lesniak, J.,Biggins, J.B.,Jeffrey, P.D.,Jiang, J.,Rajashankar, K.R.,Thorson, J.S.,Nikolov, D.B. (deposition date: 2001-04-23, release date: 2001-05-09, Last modification date: 2024-02-07)

Primary citation

Barton, W.A.,Lesniak, J.,Biggins, J.B.,Jeffrey, P.D.,Jiang, J.,Rajashankar, K.R.,Thorson, J.S.,Nikolov, D.B.
Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization.
Nat.Struct.Biol., 8:545-551, 2001

PubMed Abstract: Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.

PubMed: 11373625
DOI: 10.1038/88618

Experimental method

X-RAY DIFFRACTION (2.1 Å)