3ZGF

Crystal structure of the Fucosylgalactoside alpha N- acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with in complex with NPE caged UDP-Gal (P2(1)2(1)2(1) space group)

Summary for 3ZGF

• Entry DOI: 10.2210/pdb3zgf/pdb
• Related: 3ZGG
• Descriptor: HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: transferase, glycosyltransferases
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein: P16442
• Total number of polymer chains: 2
• Total formula weight: 70716.61

Authors

Jorgensen, R.,Batot, G.O.,Hindsgaul, O.,Tanaka, H.,Perez, S.,Imberty, A.,Breton, C.,Royant, A.,Palcic, M.M. (deposition date: 2012-12-17, release date: 2013-01-23, Last modification date: 2023-12-20)

Primary citation

Jorgensen, R.,Batot, G.,Mannerstedt, K.,Imberty, A.,Breton, C.,Hindsgaul, O.,Royant, A.,Palcic, M.M.
Structures of a Human Blood Group Glycosyltransferase in Complex with a Photo-Activatable Udp-Gal Derivative Reveal Two Different Binding Conformations
Acta Crystallogr.,Sect.F, 70:1015-, 2014

PubMed Abstract: Glycosyltransferases (GTs) catalyse the sequential addition of monosaccharides to specific acceptor molecules and play major roles in key biological processes. GTs are classified into two main families depending on the inverted or retained stereochemistry of the glycosidic bond formed during the reaction. While the mechanism of inverting enzymes is well characterized, the precise nature of retaining GTs is still a matter of much debate. In an attempt to clarify this issue, studies were initiated to identify reaction-intermediate states by using a crystallographic approach based on caged substrates. In this paper, two distinct structures of AA(Gly)B, a dual-specificity blood group synthase, are described in complex with a UDP-galactose derivative in which the O6'' atom is protected by a 2-nitrobenzyl group. The distinct conformations of the caged substrate in both structures of the enzyme illustrate the highly dynamic nature of its active site. An attempt was also made to photolyse the caged compound at low temperature, which unfortunately is not possible without damaging the uracil group as well. These results pave the way for kinetic crystallography experiments aiming at trapping and characterizing reaction-intermediate states in the mechanism of enzymatic glycosyl transfer.

PubMed: 25084373
DOI: 10.1107/S2053230X1401259X

Experimental method

X-RAY DIFFRACTION (1.701 Å)