4RIF

Landomycin Glycosyltransferase LanGT2, carbasugar substrate complex

Summary for 4RIF

• Entry DOI: 10.2210/pdb4rif/pdb
• Descriptor: Glycosyl transferase homolog, 2'-deoxy-5'-O-[(R)-{[(R)-{[(1S,3R,4R,5S)-3,4-dihydroxy-5-methylcyclohexyl]oxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]-3,4-dihydrothymidine (3 entities in total)
• Functional Keywords: gt fold, glycosyltransferase, transferase
• Biological source: Streptomyces cyanogenus
• Total number of polymer chains: 2
• Total formula weight: 81872.92

Authors

Tam, H.K.,Gerhardt, S.,Breit, B.,Bechthold, A.,Einsle, O. (deposition date: 2014-10-06, release date: 2015-01-28, Last modification date: 2024-04-03)

Primary citation

Tam, H.K.,Harle, J.,Gerhardt, S.,Rohr, J.,Wang, G.,Thorson, J.S.,Bigot, A.,Lutterbeck, M.,Seiche, W.,Breit, B.,Bechthold, A.,Einsle, O.
Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2.
Angew.Chem.Int.Ed.Engl., 54:2811-2815, 2015

PubMed Abstract: The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates.

PubMed: 25581707
DOI: 10.1002/anie.201409792

Experimental method

X-RAY DIFFRACTION (1.85 Å)