5KX6
The structure of Arabidopsis thaliana FUT1 Mutant R284K in complex with GDP
Summary for 5KX6
| Entry DOI | 10.2210/pdb5kx6/pdb |
| Related | 5KWK |
| Descriptor | Galactoside 2-alpha-L-fucosyltransferase, GUANOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | acetyl transferase, gt37, cell adhesion |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein : Q9SWH5 |
| Total number of polymer chains | 2 |
| Total formula weight | 109626.75 |
| Authors | Alahuhta, P.M.,Lunin, V.V. (deposition date: 2016-07-20, release date: 2016-09-28, Last modification date: 2024-11-20) |
| Primary citation | Urbanowicz, B.R.,Bharadwaj, V.S.,Alahuhta, M.,Pena, M.J.,Lunin, V.V.,Bomble, Y.J.,Wang, S.,Yang, J.Y.,Tuomivaara, S.T.,Himmel, M.E.,Moremen, K.W.,York, W.S.,Crowley, M.F. Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism. Plant J., 91:931-949, 2017 Cited by PubMed Abstract: The mechanistic underpinnings of the complex process of plant polysaccharide biosynthesis are poorly understood, largely because of the resistance of glycosyltransferase (GT) enzymes to structural characterization. In Arabidopsis thaliana, a glycosyl transferase family 37 (GT37) fucosyltransferase 1 (AtFUT1) catalyzes the regiospecific transfer of terminal 1,2-fucosyl residues to xyloglucan side chains - a key step in the biosynthesis of fucosylated sidechains of galactoxyloglucan. We unravel the mechanistic basis for fucosylation by AtFUT1 with a multipronged approach involving protein expression, X-ray crystallography, mutagenesis experiments and molecular simulations. Mammalian cell culture expressions enable the sufficient production of the enzyme for X-ray crystallography, which reveals the structural architecture of AtFUT1 in complex with bound donor and acceptor substrate analogs. The lack of an appropriately positioned active site residue as a catalytic base leads us to propose an atypical water-mediated fucosylation mechanism facilitated by an H-bonded network, which is corroborated by mutagenesis experiments as well as detailed atomistic simulations. PubMed: 28670741DOI: 10.1111/tpj.13628 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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