메뉴 건너뛰기




Volumn 20, Issue 5, 2011, Pages 856-866

Altered architecture of substrate binding region defines the unique specificity of UDP-GalNAc 4-epimerases

Author keywords

4 Epimerase; Galactose metabolism; Lipopolysaccharide; N acetylglucosamine; Rossmann fold

Indexed keywords

2 DEOXY LEVO ALTRURONIC ACID; GLYCAN; HEXOSE; LIPOPOLYSACCHARIDE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 79954510706     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.611     Document Type: Article
Times cited : (13)

References (44)
  • 2
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from escherichia coli determined at 2.5 A resolution
    • Bauer AJ, Rayment I, Frey PA, Holden HM (1992) The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 A resolution. Proteins 12:372-381.
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 3
    • 0037168448 scopus 로고    scopus 로고
    • New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-deoxy-l-altruronic acid in the O-antigen repeating units of Plesiomonas shigelloides O17
    • DOI 10.1021/bi026384i
    • Kowal P, Wang P (2002) New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-deoxy-l-altruronic acid in the O-antigen repeating units of Plesiomonas shigelloides O17. Biochemistry 41: 15410-15414. (Pubitemid 36008152)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15410-15414
    • Kowal, P.1    Wang, P.G.2
  • 4
    • 2542500431 scopus 로고    scopus 로고
    • Crystal structure of WbpP, a genuine UDP-N-acetylglucosamine 4-epimerase from Pseudomonas aeruginosa: Substrate specificity in UDP-hexose 4-epimerases
    • DOI 10.1074/jbc.M401642200
    • Ishiyama N, Creuzenet C, Lam JS, Berghuis AM (2004) Crystal structure of WbpP, a genuine UDP-Nacetylglucosamine 4-epimerase from Pseudomonas aeruginosa: substrate specificity in udp-hexose 4-epimerases. J Biol Chem 279:22635-22642. (Pubitemid 38679464)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22635-22642
    • Ishiyama, N.1    Creuzenet, C.2    Lam, J.S.3    Berghuis, A.M.4
  • 5
    • 0242498430 scopus 로고    scopus 로고
    • Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism
    • DOI 10.1074/jbc.R300025200
    • Holden HM, Rayment I, Thoden JB (2003) Structure and function of enzymes of the Leloir pathway for galactose metabolism. J Biol Chem 278:43885-43888. (Pubitemid 37377125)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 6
    • 34247894051 scopus 로고    scopus 로고
    • The structures of core regions from enterobacterial lipopolysaccharides - An update
    • DOI 10.1111/j.1574-6968.2007.00708.x
    • Holst O (2007) The structures of core regions from enterobacterial lipopolysaccharides-an update. FEMS Microbiol Lett 271:3-11. (Pubitemid 46701069)
    • (2007) FEMS Microbiology Letters , vol.271 , Issue.1 , pp. 3-11
    • Holst, O.1
  • 7
    • 63849263023 scopus 로고    scopus 로고
    • Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in gram-negative bacteria
    • Cuthbertson L, Mainprize IL, Naismith JH, Whitfield C (2009) Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in gram-negative bacteria. Microbiol Mol Biol Rev 73: 155-177.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 155-177
    • Cuthbertson, L.1    Mainprize, I.L.2    Naismith, J.H.3    Whitfield, C.4
  • 8
    • 0031036833 scopus 로고    scopus 로고
    • Regulation of O-antigen chain length is required for Shigella flexneri virulence
    • Van Den Bosch L, Manning PA, Morona R (1997) Regulation of O-antigen chain length is required for Shigella flexneri virulence. Mol Microbiol 23:765-775. (Pubitemid 27072937)
    • (1997) Molecular Microbiology , vol.23 , Issue.4 , pp. 765-775
    • Van Den Bosch, L.1    Manning, P.A.2    Morona, R.3
  • 9
    • 33645214751 scopus 로고    scopus 로고
    • Altering the length of the lipopolysaccharide O antigen has an impact on the interaction of salmonella enterica serovar typhimurium with macrophages and complement
    • Murray GL, Attridge SR, Morona R (2006) Altering the length of the lipopolysaccharide O antigen has an impact on the interaction of Salmonella enterica serovar Typhimurium with macrophages and complement. J Bacteriol 188:2735-2739.
    • (2006) J Bacteriol , vol.188 , pp. 2735-2739
    • Murray, G.L.1    Attridge, S.R.2    Morona, R.3
  • 10
    • 0030973246 scopus 로고    scopus 로고
    • Effect of mutations in Shigella flexneri chromosomal and plasmid-encoded lipopolysaccharide genes on invasion and serum resistance
    • Hong M, Payne SM (1997) Effect of mutations in Shigella flexneri chromosomal and plasmid-encoded lipopolysaccharide genes on invasion and serum resistance. Mol Microbiol 24:779-791. (Pubitemid 27229723)
    • (1997) Molecular Microbiology , vol.24 , Issue.4 , pp. 779-791
    • Hong, M.1    Payne, S.M.2
  • 11
    • 0033073396 scopus 로고    scopus 로고
    • Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia
    • Wohlers T, Christacos N, Harreman M, Fridovich-Keil J (1999) Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia. Am J Human Gen 64:462-470. (Pubitemid 129500528)
    • (1999) American Journal of Human Genetics , vol.64 , Issue.2 , pp. 462-470
    • Wohlers, T.M.1    Christacos, N.C.2    Harreman, M.T.3    Fridovich-Keil, J.L.4
  • 12
    • 0031669072 scopus 로고    scopus 로고
    • Human UDP-galactose 4' epimerase (GALE) gene and identification of five missense mutations in patients with epimerase-deficiency galactosemia
    • DOI 10.1006/mgme.1997.2645
    • Maceratesi P, Daude N, Dallapiccola B, Novelli G, Allen R, Okano Y, Reichardt J (1998) Human UDP-galactose 4' epimerase (GALE) gene and identification of five missense mutations in patients with epimerasedeficiency galactosemia. Mol Genet Metab 63:26-30. (Pubitemid 28455923)
    • (1998) Molecular Genetics and Metabolism , vol.63 , Issue.1 , pp. 26-30
    • Maceratesi, P.1    Daude, N.2    Dallapiccola, B.3    Novelli, G.4    Allen, R.5    Okano, Y.6    Reichardt, J.7
  • 13
    • 0000290994 scopus 로고
    • The enzymes of the galactose operon in escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase
    • Wilson DB, Hogness DS (1964) The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase. J Biol Chem 239:2469-2481.
    • (1964) J Biol Chem , vol.239 , pp. 2469-2481
    • Wilson, D.B.1    Hogness, D.S.2
  • 14
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
    • DOI 10.1021/bi000215l
    • Thoden J, Wohlers T, Fridovich-Keil J, Holden H (2000) Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP- galactose 4-epimerase. Biochemistry 39:5691-5701. (Pubitemid 30307957)
    • (2000) Biochemistry , vol.39 , Issue.19 , pp. 5691-5701
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 15
    • 0030832007 scopus 로고    scopus 로고
    • Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4- epimerase from Escherichia coli
    • DOI 10.1021/bi970430a
    • Liu Y, Thoden JB, Kim J, Berger E, Gulick AM, Ruzicka FJ, Holden HM, Frey PA (1997) Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 36: 10675-10684. (Pubitemid 27382557)
    • (1997) Biochemistry , vol.36 , Issue.35 , pp. 10675-10684
    • Liu, Y.1    Thoden, J.B.2    Kim, J.3    Berger, E.4    Gulick, A.M.5    Ruzicka, F.J.6    Holden, H.M.7    Frey, P.A.8
  • 16
    • 22144437306 scopus 로고    scopus 로고
    • Towards a better understanding of the substrate specificity of the UDP-N-acetylglucosamine C4 epimerase WbpP
    • DOI 10.1042/BJ20050263
    • Demendi M, Ishiyama N, Lam JS, Berghuis AM, Creuzenet C (2005) Towards a better understanding of the substrate specificity of the UDP-N-acetylglucosamine C4 epimerase WbpP. Biochem J 389:173-180. (Pubitemid 40978020)
    • (2005) Biochemical Journal , vol.389 , Issue.1 , pp. 173-180
    • Demendi, M.1    Ishiyama, N.2    Lam, J.S.3    Berghuis, A.M.4    Creuzenet, C.5
  • 17
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst A47:392-400.
    • (1991) Acta Cryst , vol.47 A , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 20
    • 0037178867 scopus 로고    scopus 로고
    • Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks
    • DOI 10.1074/jbc.M204413200
    • Thoden JB, Henderson JM, Fridovich-Keil JL, Holden HM (2002) Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks. J Biol Chem 277:27528-27534. (Pubitemid 34959955)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27528-27534
    • Thoden, J.B.1    Henderson, J.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 21
    • 33751250543 scopus 로고    scopus 로고
    • Biochemical characterization of UDP-GlcNAc/Glc 4-epimerase from Escherichia coli O86:B7
    • DOI 10.1021/bi0612770
    • Guo H, Li L, Wang PG (2006) Biochemical characterization of UDP-GlcNAc/Glc 4-epimerase from Escherichia coli O86:B7. Biochemistry 45:13760-13768. (Pubitemid 44788745)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13760-13768
    • Guo, H.1    Li, L.2    Wang, P.G.3
  • 23
    • 0037327814 scopus 로고    scopus 로고
    • High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: A potential target for structure-based development of novel trypanocides
    • DOI 10.1016/S0166-6851(02)00243-8, PII S0166685102002438
    • Shaw MP, Bond CS, Roper JR, Gourley DG, Ferguson MAJ, Hunter WN (2003) High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4'-epimerase: a potential target for structure-based development of novel trypanocides. Mol Biochem Parasitol 126: 173-180. (Pubitemid 36255616)
    • (2003) Molecular and Biochemical Parasitology , vol.126 , Issue.2 , pp. 173-180
    • Shaw, M.P.1    Bond, C.S.2    Roper, J.R.3    Gourley, D.G.4    Ferguson, M.A.J.5    Hunter, W.N.6
  • 25
    • 76249117733 scopus 로고    scopus 로고
    • A novel epimerase that converts GlcNAc-PP-undecaprenol to GalNAc-P-P-undecaprenol in escherichia coli O157
    • Rush JS, Alaimo C, Robbiani R, Wacker M, Waechter CJ (2010) A novel epimerase that converts GlcNAc-PP-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157. J Biol Chem 285:1671-1680.
    • (2010) J Biol Chem , vol.285 , pp. 1671-1680
    • Rush, J.S.1    Alaimo, C.2    Robbiani, R.3    Wacker, M.4    Waechter, C.J.5
  • 26
    • 0031936811 scopus 로고    scopus 로고
    • Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques
    • DOI 10.1107/S0907444997005374
    • Chayen NE (1998) Comparative studies of protein crystallization by vapour-diffusion and microbatch techniques. Acta Cryst D54:8-15. (Pubitemid 28111113)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.1 , pp. 8-15
    • Chayen, N.E.1
  • 27
    • 4344718651 scopus 로고    scopus 로고
    • Practical aspects of using the microbatch method in screening conditions for protein crystallization
    • DOI 10.1016/j.ymeth.2004.03.023, PII S1046202304001148
    • D'Arcy A, Sweeney AM, Haber A (2004) Practical aspects of using the microbatch method in screening conditions for protein crystallization. Methods 34: 323-328. (Pubitemid 39119816)
    • (2004) Methods , vol.34 , Issue.3 , pp. 323-328
    • D'Arcy, A.1    Sweeney, A.M.2    Haber, A.3
  • 31
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 14244263595 scopus 로고    scopus 로고
    • A single bifunctional UDP-GlcNAc/Glc 4-epimerase supports the synthesis of three cell surface glycoconjugates in campylobacter jejuni
    • Bernatchez S, Szymanski C, Ishiyama N, Li J, Jarrell H, Lau P, Berghuis A, Young N, Wakarchuk W (2005) A single bifunctional UDP-GlcNAc/Glc 4-epimerase supports the synthesis of three cell surface glycoconjugates in Campylobacter jejuni. J Biol Chem 280:4792.
    • (2005) J Biol Chem , vol.280 , pp. 4792
    • Bernatchez, S.1    Szymanski, C.2    Ishiyama, N.3    Li, J.4    Jarrell, H.5    Lau, P.6    Berghuis, A.7    Young, N.8    Wakarchuk, W.9
  • 35
    • 0034705422 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6
    • DOI 10.1074/jbc.M001171200
    • Creuzenet C, Belanger M, Wakarchuk WW, Lam JS (2000) Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6. J Biol Chem 275:19060-19067. (Pubitemid 30422873)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19060-19067
    • Creuzenet, C.1    Belanger, M.2    Wakarchuk, W.W.3    Lam, J.S.4
  • 36
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 37
    • 0029877040 scopus 로고    scopus 로고
    • Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli
    • DOI 10.1021/bi952715y
    • Thoden JB, Frey PA, Holden HM (1996) Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli. Biochemistry 35:2557-2566. (Pubitemid 26098763)
    • (1996) Biochemistry , vol.35 , Issue.8 , pp. 2557-2566
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3
  • 38
    • 0035805630 scopus 로고    scopus 로고
    • Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site
    • Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM (2001) Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site. J Biol Chem 276:15131-15136.
    • (2001) J Biol Chem , vol.276 , pp. 15131-15136
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 39
    • 74249106219 scopus 로고    scopus 로고
    • I-TASSER: Fully automated protein structure prediction in CASP8
    • Zhang Y (2009) I-TASSER: fully automated protein structure prediction in CASP8. Proteins 77(Suppl 9): 100-113.
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 100-113
    • Zhang, Y.1
  • 41
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • DOI 10.1093/nar/gkl282
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J (2006) CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res 34:W116-W118. (Pubitemid 44529746)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS.
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 43
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • DOI 10.1016/j.jsb.2006.06.010, PII S1047847706001948, Software Tools for Macromolecular Microscopy
    • Goddard TD, Huang CC, Ferrin TE (2007) Visualizing density maps with UCSF Chimera. J Struct Biol 157: 281-287. (Pubitemid 44880787)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 44
    • 79954533743 scopus 로고    scopus 로고
    • Scientific visualizations with POV-Ray
    • Orf L (2004) Scientific visualizations with POV-Ray. Linux J 2004:2.
    • (2004) Linux J , vol.2004 , pp. 2
    • Orf, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.