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Volumn 4, Issue 10, 2009, Pages

Crystal structure of the N-acetylmannosamine kinase domain of GNE

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; N ACETYLMANNOSAMINE KINASE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE; CARBOHYDRATE; EPIMERASE; LIGAND; UDP ACETYLGLUCOSAMINE 2 EPIMERASE; UDP ACETYLGLUCOSAMINE-2-EPIMERASE;

EID: 70449359887     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007165     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 0032443144 scopus 로고    scopus 로고
    • Structure, function and metabolism of sialic acids
    • Traving C, Schauer R (1998) Structure, function and metabolism of sialic acids. Cell Mol Life Sci 54: 1330-1349.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 1330-1349
    • Traving, C.1    Schauer, R.2
  • 4
    • 0033809048 scopus 로고    scopus 로고
    • Bacterial genetics and human immunity to group B streptococci
    • Adderson EE, Takahashi S, Bohnsack JF (2000) Bacterial genetics and human immunity to group B streptococci. Mol Genet Metab 71: 451-454.
    • (2000) Mol Genet Metab , vol.71 , pp. 451-454
    • Adderson, E.E.1    Takahashi, S.2    Bohnsack, J.F.3
  • 5
    • 51249120074 scopus 로고    scopus 로고
    • Association between faecal shedding of feline coronavirus and serum alpha1-acid glycoprotein sialylation
    • Paltrinieri S, Gelain ME, Ceciliani F, Ribera AM, Battilani M (2008) Association between faecal shedding of feline coronavirus and serum alpha1-acid glycoprotein sialylation. J Feline Med Surg 10: 514-518.
    • (2008) J Feline Med Surg , vol.10 , pp. 514-518
    • Paltrinieri, S.1    Gelain, M.E.2    Ceciliani, F.3    Ribera, A.M.4    Battilani, M.5
  • 6
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • Angata T, Varki A (2002) Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem Rev 102: 439-469.
    • (2002) Chem Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 8
    • 0028000790 scopus 로고
    • Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria
    • Titgemeyer F, Reizer J, Reizer A, Saier MH, Jr. (1994) Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology 140 (Pt 9): 2349-2354.
    • (1994) Microbiology , vol.140 , Issue.PART 9 , pp. 2349-2354
    • Titgemeyer, F.1    Reizer, J.2    Reizer, A.3    Saier Jr., M.H.4
  • 9
    • 64149117237 scopus 로고    scopus 로고
    • Biochemical characterization of human and murine isoforms of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE)
    • Reinke SO, Eidenschink C, Jay CM, Hinderlich S (2009) Biochemical characterization of human and murine isoforms of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE). Glycoconj J 26: 415-422.
    • (2009) Glycoconj J , vol.26 , pp. 415-422
    • Reinke, S.O.1    Eidenschink, C.2    Jay, C.M.3    Hinderlich, S.4
  • 10
    • 0033215205 scopus 로고    scopus 로고
    • Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/ N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments
    • Effertz K, Hinderlich S, Reutter W (1999) Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/ N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments. J Biol Chem 274: 28771-28778.
    • (1999) J Biol Chem , vol.274 , pp. 28771-28778
    • Effertz, K.1    Hinderlich, S.2    Reutter, W.3
  • 11
    • 33644689755 scopus 로고    scopus 로고
    • Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy
    • Penner J, Mantey LR, Elgavish S, Ghaderi D, Cirak S, et al. (2006) Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy. Biochemistry 45: 2968-2977.
    • (2006) Biochemistry , vol.45 , pp. 2968-2977
    • Penner, J.1    Mantey, L.R.2    Elgavish, S.3    Ghaderi, D.4    Cirak, S.5
  • 12
    • 0039546871 scopus 로고    scopus 로고
    • Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme
    • Seppala R, Lehto VP, Gahl WA (1999) Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. Am J Hum Genet 64: 1563-1569.
    • (1999) Am J Hum Genet , vol.64 , pp. 1563-1569
    • Seppala, R.1    Lehto, V.P.2    Gahl, W.A.3
  • 13
    • 17944366749 scopus 로고    scopus 로고
    • The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy
    • Eisenberg I, Avidan N, Potikha T, Hochner H, Chen M, et al. (2001) The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat Genet 29: 83-87.
    • (2001) Nat Genet , vol.29 , pp. 83-87
    • Eisenberg, I.1    Avidan, N.2    Potikha, T.3    Hochner, H.4    Chen, M.5
  • 14
    • 23844532942 scopus 로고    scopus 로고
    • The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli
    • Schiefner A, Gerber K, Seitz S, Welte W, Diederichs K, et al. (2005) The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli. J Biol Chem 280: 29073-29079.
    • (2005) J Biol Chem , vol.280 , pp. 29073-29079
    • Schiefner, A.1    Gerber, K.2    Seitz, S.3    Welte, W.4    Diederichs, K.5
  • 15
    • 36749023905 scopus 로고    scopus 로고
    • Divergent evolution of function in the ROK sugar kinase superfamily: Role of enzyme loops in substrate specificity
    • Larion M, Moore LB, Thompson SM, Miller BG (2007) Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity. Biochemistry 46: 13564-13572.
    • (2007) Biochemistry , vol.46 , pp. 13564-13572
    • Larion, M.1    Moore, L.B.2    Thompson, S.M.3    Miller, B.G.4
  • 16
    • 0027463380 scopus 로고
    • A new ATP-binding fold in actin, hexokinase and Hsc70
    • Holmes KC, Sander C, Valencia A (1993) A new ATP-binding fold in actin, hexokinase and Hsc70. Trends Cell Biol 3: 53-59.
    • (1993) Trends Cell Biol , vol.3 , pp. 53-59
    • Holmes, K.C.1    Sander, C.2    Valencia, A.3
  • 17
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sander C, Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A 89: 7290-7294.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 18
    • 10944220454 scopus 로고    scopus 로고
    • Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/ N-acetylmannosamine kinase
    • Blume A, Weidemann W, Stelzl U, Wanker EE, Lucka L, et al. (2004) Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/ N-acetylmannosamine kinase. Biochem J 384: 599-607.
    • (2004) Biochem J , vol.384 , pp. 599-607
    • Blume, A.1    Weidemann, W.2    Stelzl, U.3    Wanker, E.E.4    Lucka, L.5
  • 19
    • 34248205764 scopus 로고    scopus 로고
    • Evidence for dynamic interplay of different oligomeric states of UDP-N-acetylglucosamine 2-epimerase/N-acetyalmannosamine kinase by biophysical methods
    • Ghaderi D, Strauss HM, Reinke S, Cirak S, Reutter W, et al. (2007) Evidence for dynamic interplay of different oligomeric states of UDP-N-acetylglucosamine 2-epimerase/N-acetyalmannosamine kinase by biophysical methods. J Mol Biol 369: 746-758.
    • (2007) J Mol Biol , vol.369 , pp. 746-758
    • Ghaderi, D.1    Strauss, H.M.2    Reinke, S.3    Cirak, S.4    Reutter, W.5
  • 20
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 3242887315 scopus 로고    scopus 로고
    • FATCAT: A web server for flexible structure comparison and structure similarity searching
    • Ye Y, Godzik A (2004) FATCAT: a web server for flexible structure comparison and structure similarity searching. Nucleic Acids Res 32: W582-W585.
    • (2004) Nucleic Acids Res , vol.32
    • Ye, Y.1    Godzik, A.2
  • 22
    • 41649085020 scopus 로고    scopus 로고
    • Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration
    • Nam TW, Jung HI, An YJ, Park YH, Lee SH, et al. (2008) Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Proc Natl Acad Sci U S A 105: 3751-3756.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3751-3756
    • Nam, T.W.1    Jung, H.I.2    An, Y.J.3    Park, Y.H.4    Lee, S.H.5
  • 23
    • 4944262604 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose
    • Lunin VV, Li Y, Schrag JD, Iannuzzi P, Cygler M, et al. (2004) Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose. J Bacteriol 186: 6915-6927.
    • (2004) J Bacteriol , vol.186 , pp. 6915-6927
    • Lunin, V.V.1    Li, Y.2    Schrag, J.D.3    Iannuzzi, P.4    Cygler, M.5
  • 24
    • 70249085865 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathy: A decade of progress
    • doi:10.1016/ j.bbadis.2009.07.001
    • Huizing M, Krasnewich DM (2009) Hereditary inclusion body myopathy: a decade of progress. Biochim Biophys Acta doi:10.1016/ j.bbadis.2009.07.001.
    • (2009) Biochim Biophys Acta
    • Huizing, M.1    Krasnewich, D.M.2
  • 25
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger TC (2003) SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol 374: 22-37.
    • (2003) Methods Enzymol , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 26
  • 29
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis IW, Murray LW, Richardson JS, Richardson DC (2004) MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res 32: W615-W619.
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 30
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 31
    • 2942522721 scopus 로고    scopus 로고
    • ASAView: Database and tool for solvent accessibility representation in proteins
    • Ahmad S, Gromiha M, Fawareh H, Sarai A (2004) ASAView: database and tool for solvent accessibility representation in proteins. BMC Bioinformatics 5: 51.
    • (2004) BMC Bioinformatics , vol.5 , pp. 51
    • Ahmad, S.1    Gromiha, M.2    Fawareh, H.3    Sarai, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.