Skip to main content

Structures of NodZ α1,6‐fucosyltransferase in complex with GDP and GDP‐fucose

Buy Article:

$51.00 plus tax (Refund Policy)


Rhizobial NodZ α1,6‐fucosyltransferase (α1,6‐FucT) catalyzes the transfer of the fucose (Fuc) moiety from guanosine 5′‐diphosphate‐β‐l‐fucose to the reducing end of the chitin oligosaccharide core during Nod‐factor (NF) biosynthesis. NF is a key signalling molecule required for successful symbiosis with a legume host for atmospheric nitrogen fixation. To date, only two α1,6‐FucT structures have been determined, both without any donor or acceptor molecule that could highlight the structural background of the catalytic mechanism. Here, the first crystal structures of α1,6‐FucT in complex with its substrate GDP‐Fuc and with GDP, which is a byproduct of the enzymatic reaction, are presented. The crystal of the complex with GDP‐Fuc was obtained through soaking of native NodZ crystals with the ligand and its structure has been determined at 2.35 Å resolution. The fucose residue is exposed to solvent and is disordered. The enzyme–product complex crystal was obtained by cocrystallization with GDP and an acceptor molecule, penta‐N‐acetyl‐l‐glucosamine (penta‐NAG). The structure has been determined at 1.98 Å resolution, showing that only the GDP molecule is present in the complex. In both structures the ligands are located in a cleft formed between the two domains of NodZ and extend towards the C‐terminal domain, but their conformations differ significantly. The structures revealed that residues in three regions of the C‐terminal domain, which are conserved among α1,2‐, α1,6‐ and protein O‐fucosyltransferases, are involved in interactions with the sugar‐donor molecule. There is also an interaction with the side chain of Tyr45 in the N‐terminal domain, which is very unusual for a GT‐B‐type glycosyltransferase. Only minor conformational changes of the protein backbone are observed upon ligand binding. The only exception is a movement of the loop located between strand βC2 and helix αC3. In addition, there is a shift of the αC3 helix itself upon GDP‐Fuc binding.

Document Type: Research Article


Publication date: February 1, 2012


Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more