4RII

Chimeric Glycosyltransferase LanGT2S8Ac, TDP complex

Summary for 4RII

Entry DOI	10.2210/pdb4rii/pdb
Descriptor	Glycosyl transferase homolog,Glycosyl transferase, THYMIDINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	gt fold, c-glycosylating glycosyltransferase, transferase
Biological source	Streptomyces cyanogenus More
Total number of polymer chains	2
Total formula weight	81734.99
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation