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C.P.C. Chiu, A.G. Watts, L.L. Lairson, M. Gilbert, D. Lim, W.W. Wakarchuk, S.G. Withers, and N.C.J. Strynadka Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog Nat Struct Mol Biol 11 2004 163 170 Cell-surface sialic acid is one of the most important glycosylations in nature. This paper reports the first sialyltransferase structure determination and was consequently one of the American Chemical Society 'Chemical Highlights' of 2004. The enzyme transfers sialic acid to cell-surface glycoproteins and glycolipids. It has an unusual deviation from the canonical GT-A fold, with the donor interactions revealed through crystallisation with a non-transferrable DMP-sialic acid mimic.
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L.C. Pedersen, J. Dong, F. Taniguchi, H. Kitagawa, J.M. Krahn, L.G. Pedersen, K. Sugahara, and M. Negishi Crystal structure of an alpha 1,4-N- acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis J Biol Chem 278 2003 14420 14428 A fine structure determination and very interesting piece of scientific writing. All those working on retaining glycosyltransferases should read this paper, which reports the first structures of members of the exostosin gene family and provides an important structural dissection of the mechanisms of heparan synthesis.
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J. Flint, E. Taylor, M. Yang, D.N. Bolam, L.E. Tailford, C. Martinez-Flietes, E.J. Dodson, B.G. Davis, H.J. Gilbert, and G.J. Davies Structural dissection and high-throughput screening of mannosylglycerate synthase Nat Struct Mol Biol 12 2005 608 614 This work suggests one possible route to the functional dissection of glycosyltransferase activity. Three-dimensional structure is mute without solution characterisation of activity. Nowhere is this more true than in glycosyltransferase studies, not least because the two known folds are also adopted by enzymes that are not glycosyltransferases.
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Nat Struct Mol Biol
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Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9Å resolution
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F. Vincent, S.J. Charnock, K.H.G. Verschueren, J.P. Turkenburg, D.J. Scott, W.A. Offen, S. Roberts, G. Pell, H.J. Gilbert, and G.J. Davies Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9Å resolution J Mol Biol 330 2003 593 606
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The crystal structure of feruloyl esterase a from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family
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J.A. Hermoso, J. Sanz-Aparicio, R. Molina, N. Juge, R. Gonzalez, and C.B. Faulds The crystal structure of feruloyl esterase a from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family J Mol Biol 338 2004 495 506
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J. Jenkins, O. Mayans, D. Smith, K. Worboys, and R.W. Pickersgill Three-dimensional structure of Erwinia chrysanthemi pectin methyl esterase reveals a novel esterase active site J Mol Biol 305 2001 951 960
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M. Hernick, and C.A. Fierke Zinc hydrolases: the mechanisms of zinc-dependent deacetylases Arch Biochem Biophys 433 2005 71 84
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Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis
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D.A. Whittington, K.M. Rusche, H. Shin, C.A. Fierke, and D.W. Chistianson Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis Proc Natl Acad Sci USA 100 2003 8146 8150
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Structure of the lpxC deacetylase with a bound substrate analog inhibitor
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B.E. Coggins, X. Li, A.L. McClerren, O. Hindsgaul, C.R.H. Raetz, and P. Zhou Structure of the lpxC deacetylase with a bound substrate analog inhibitor Nat Struct Biol 10 2003 645 651
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0345306583
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The crystal structure of 1-d-myo-inosityl-2-acetamido-2-deoxy-alpha-d- glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold
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J.T. Maynes, C. Garen, M.M. Cherney, G. Newton, D. Arad, Y. Av-Gay, R.C. Fahey, and M.N.G. James The crystal structure of 1-d-myo-inosityl-2-acetamido-2- deoxy-alpha-d-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold J Biol Chem 278 2003 47166 47170
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50
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Structure and metal-dependent mechanism of peptidoglycan deacetylase, a Streptococcal virulence factor
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in press.
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Blair DE, Schuttelkopf AW, MacRae JA, van Aalten DMF: Structure and metal-dependent mechanism of peptidoglycan deacetylase, a Streptococcal virulence factor. Proc Natl Acad Sci USA 2005, in press.
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Proc Natl Acad Sci USA
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Blair, D.E.1
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51
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1642576068
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The 3-D structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: A member of the urease superfamily
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F. Vincent, D. Yates, E. Garman, G.J. Davies, and J.A. Brannigan The 3-D structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily J Biol Chem 279 2004 2809 2816
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Carbohydrate-binding modules: Fine tuning polysaccharide recognition
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A.B. Boraston, D.N. Bolam, H.J. Gilbert, and G.J. Davies Carbohydrate-binding modules: fine tuning polysaccharide recognition Biochem J 382 2004 769 781 A long-overdue review of CBMs, their three-dimensional structures and their mechanism of binding.
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Biochem J
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Boraston, A.B.1
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53
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15744367514
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Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
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G. Vaaje-Kolstad, D.R. Houston, A.H.K. Riemen, V.G.H. Eijsink, and D.M.F. van Aalten Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21 J Biol Chem 280 2005 11313 11319 This elegant work clearly demonstrates a highly significant enhancement of enzyme activity when the CBM is added 'in trans'. Furthermore, electron micrographs show clear physical impact on the substrate by the chitin-binding module. A rare piece of unambiguous work in this controversial area.
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J Biol Chem
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Vaaje-Kolstad, G.1
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54
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0842346119
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L. McCartney, H.J. Gilbert, D.N. Bolam, A.B. Boraston, and J.P. Knox Glycoside hydrolase carbohydrate-binding modules as molecular probes for the analysis of plant cell wall polymers Anal Biochem 326 2004 49 54 The fact that many prokaryotes harness very different families of CBMs on their enzymes has long been confusing. This work not only reveals that different CBM families target different 'substructures' of plant cell-wall polysaccharides, but also provides a method to exploit this specificity for the analysis of cellular 'glyco-architecture'.
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Anal Biochem
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McCartney, L.1
Gilbert, H.J.2
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0041422487
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A chemical approach for identifying O-GlcNAc-modified proteins in cells
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D.J. Vocadlo, H.C. Hang, E.J. Kim, J.A. Hanover, and C.R. Bertozzi A chemical approach for identifying O-GlcNAc-modified proteins in cells Proc Natl Acad Sci USA 100 2003 9116 9121 An elegant 'chemical biology' approach to analysing the massively important O-GlcNAc modification in eukaryotes. One can expect to see similar approaches harnessed to study many of the complex glycosylation reactions in the cell.
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Proc Natl Acad Sci USA
, vol.100
, pp. 9116-9121
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Vocadlo, D.J.1
Hang, H.C.2
Kim, E.J.3
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Bertozzi, C.R.5
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A strategy for functional proteomic analysis of glycosidase activity from cell lysates
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D.J. Vocadlo, and C.R. Bertozzi A strategy for functional proteomic analysis of glycosidase activity from cell lysates Angew Chem Int Ed Engl 43 2004 5338 5342
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O-GlcNAcase uses substrate-assisted catalysis - Kinetic analysis and development of highly selective mechanism-inspired inhibitors
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M.S. Macauley, G.E. Whitworth, A.W. Debowski, D. Chin, and D.J. Vocadlo O-GlcNAcase uses substrate-assisted catalysis - kinetic analysis and development of highly selective mechanism-inspired inhibitors J Biol Chem 280 2005 25313 25322 Again a vision of the future using the O-GlcNAc modification as an example. A panel of inhibitors both define the reaction mechanism and allow specific intervention.
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(2005)
J Biol Chem
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MacAuley, M.S.1
Whitworth, G.E.2
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58
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0037865396
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Mapping the conformational itinerary of β-glycosidases by X-ray crystallography
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G.J. Davies, V.M.-A. Ducros, A. Varrot, and D.L. Zechel Mapping the conformational itinerary of β-glycosidases by X-ray crystallography Biochem Soc Trans 31 2003 523 527
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Biochem Soc Trans
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Davies, G.J.1
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N. Sharon The conquest of the last frontier of molecular and cell biology Biochimie 83 2001 555
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