Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Autor: Dong, YY, Wang, H, Pike, ACW, Cochrane, SA, Hamedzadeh, S, Wyszyński, FJ, Bushell, SR, Royer, SF, Widdick, DA, Sajid, A, Boshoff, HI, Park, Y, Lucas, R, Liu, W-M, Lee, SS, Machida, T, Minall, L, Mehmood, S, Belaya, K, Liu, W-W, Chu, A, Shrestha, L, Mukhopadhyay, SMM, Strain-Damerell, C, Chalk, R, Burgess-Brown, NA, Bibb, MJ, Barry, CE, Robinson, CV, Beeson, D, Davis, BG, Carpenter, EP

Publikováno v: Cell
Dong, Y Y, Wang, H, Pike, A C W, Cochrane, S A, Hamedzadeh, S, Wyszynski, F, Bushell, S, Royer, S F, Widdick, D A, Sajid, A, Boshoff, H I, Park, Y, Lucas, R, Liu, W-M, Lee, S S, Machida, T, Minall, L, Mehmood, S, Belaya, K, Liu, W-W, Chu, A, Shrestha, L, Mukhopadhyay, S M M, Strain-Damerell, C, Chalk, R, Burgess-Brown, N A, Bibb, M, Barry 3rd, C, Robinson, C, Beeson, D, Davis, B & Carpenter, E P 2018, ' Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design ', Cell, vol. 175, pp. 1045-1058 . https://doi.org/10.1016/j.cell.2018.10.037

Summary Protein N-glycosylation is a widespread post-translational modification. The first committed step in this process is catalysed by dolichyl-phosphate N-acetylglucosamine-phosphotransferase DPAGT1 (GPT/E.C. 2.7.8.15). Missense DPAGT1 variants c

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https://ora.ox.ac.uk/objects/uuid:515d9416-1e72-4e91-87e4-39eb4f426368

Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.

Autor: Dong YY; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Wang H; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Pike ACW; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Cochrane SA; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK; School of Chemistry and Chemical Engineering, Queen's University, Belfast, UK., Hamedzadeh S; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Wyszyński FJ; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Bushell SR; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Royer SF; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Widdick DA; Department of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK., Sajid A; Tuberculosis Research Section, Laboratory of Clinical Immunology and Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA., Boshoff HI; Tuberculosis Research Section, Laboratory of Clinical Immunology and Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA., Park Y; Tuberculosis Research Section, Laboratory of Clinical Immunology and Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA., Lucas R; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Liu WM; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Lee SS; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Machida T; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Minall L; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Mehmood S; Department of Chemistry, Oxford, OX1 3QZ, UK., Belaya K; Neurosciences Group, Nuffield Department of Clinical Neuroscience, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK., Liu WW; Neurosciences Group, Nuffield Department of Clinical Neuroscience, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK., Chu A; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Shrestha L; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Mukhopadhyay SMM; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Strain-Damerell C; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Chalk R; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Burgess-Brown NA; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK., Bibb MJ; Department of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, UK., Barry Iii CE; Tuberculosis Research Section, Laboratory of Clinical Immunology and Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA., Robinson CV; Department of Chemistry, Oxford, OX1 3QZ, UK., Beeson D; Neurosciences Group, Nuffield Department of Clinical Neuroscience, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK., Davis BG; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK. Electronic address: Ben.Davis@chem.ox.ac.uk., Carpenter EP; Structural Genomics Consortium, University of Oxford, Oxford, OX3 7DQ, UK. Electronic address: liz.carpenter@sgc.ox.ac.uk.

Publikováno v: Cell [Cell] 2018 Nov 01; Vol. 175 (4), pp. 1045-1058.e16.

Syntheses of 2-keto-3-deoxy-D-xylonate and 2-keto-3-deoxy-L-arabinonate as stereochemical probes for demonstrating the metabolic promiscuity of Sulfolobus solfataricus towards D-xylose and L-arabinose.

Autor: Archer RM; Department of Chemistry, University of Bath, Bath BA2 7AY, UK., Royer SF, Mahy W, Winn CL, Danson MJ, Bull SD

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2013 Feb 18; Vol. 19 (8), pp. 2895-902. Date of Electronic Publication: 2013 Jan 11.