메뉴 건너뛰기




Volumn 82, Issue 7, 2014, Pages 1519-1526

Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc

Author keywords

Allosteric; Epimerization; Evolution; Rossmann fold; UDP ManNAc

Indexed keywords

URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE; ARCHAEAL PROTEIN; EPIMERASE; UDP ACETYLGLUCOSAMINE-2-EPIMERASE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 84902152041     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24516     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0017893191 scopus 로고
    • Enzymatic formation of uridine diphosphate N-acetyl-d-mannosamine
    • Kawamura T, Kimura M, Yamamori S, Ito E. Enzymatic formation of uridine diphosphate N-acetyl-d-mannosamine. J Biol Chem 1978;253(10):3595-3601.
    • (1978) J Biol Chem , vol.253 , Issue.10 , pp. 3595-3601
    • Kawamura, T.1    Kimura, M.2    Yamamori, S.3    Ito, E.4
  • 2
    • 0018787224 scopus 로고
    • Enzymatic synthesis of uridine diphosphate N-acetyl-d-mannosaminuronic acid
    • Kawamura T, Ishimoto N, Ito E. Enzymatic synthesis of uridine diphosphate N-acetyl-d-mannosaminuronic acid. J Biol Chem 1979;254(17):8457-8465.
    • (1979) J Biol Chem , vol.254 , Issue.17 , pp. 8457-8465
    • Kawamura, T.1    Ishimoto, N.2    Ito, E.3
  • 3
    • 0015837746 scopus 로고
    • Immunological properties of teichoic acids
    • Knox KW, Wicken AJ. Immunological properties of teichoic acids. Bacteriol Rev 1973;37(2):215-257.
    • (1973) Bacteriol Rev , vol.37 , Issue.2 , pp. 215-257
    • Knox, K.W.1    Wicken, A.J.2
  • 4
    • 0036063920 scopus 로고    scopus 로고
    • Characterization of a Bacillus subtilis thermosensitive teichoic acid-deficient mutant: gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-epimerase
    • Soldo B, Lazarevic V, Pooley HM, Karamata D. Characterization of a Bacillus subtilis thermosensitive teichoic acid-deficient mutant: gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-epimerase. J Bacteriol 2002;184(15):4316-4320.
    • (2002) J Bacteriol , vol.184 , Issue.15 , pp. 4316-4320
    • Soldo, B.1    Lazarevic, V.2    Pooley, H.M.3    Karamata, D.4
  • 5
    • 0032816695 scopus 로고    scopus 로고
    • Staphylococcus aureus cap5P encodes a UDP-N-acetylglucosamine 2-epimerase with functional redundancy
    • Kiser KB, Bhasin N, Deng L, Lee JC. Staphylococcus aureus cap5P encodes a UDP-N-acetylglucosamine 2-epimerase with functional redundancy. J Bacteriol 1999;181(16):4818-4824.
    • (1999) J Bacteriol , vol.181 , Issue.16 , pp. 4818-4824
    • Kiser, K.B.1    Bhasin, N.2    Deng, L.3    Lee, J.C.4
  • 6
    • 38949105849 scopus 로고    scopus 로고
    • A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases
    • Velloso LM, Bhaskaran SS, Schuch R, Fischetti VA, Stebbins CE. A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases. EMBO Rep 2008;9(2):199-205.
    • (2008) EMBO Rep , vol.9 , Issue.2 , pp. 199-205
    • Velloso, L.M.1    Bhaskaran, S.S.2    Schuch, R.3    Fischetti, V.A.4    Stebbins, C.E.5
  • 7
    • 0036005636 scopus 로고    scopus 로고
    • Understanding nature's strategies for enzyme-catalyzed racemization and epimerization
    • Tanner ME. Understanding nature's strategies for enzyme-catalyzed racemization and epimerization. Acc Chem Res 2002;35(4):237-246.
    • (2002) Acc Chem Res , vol.35 , Issue.4 , pp. 237-246
    • Tanner, M.E.1
  • 8
    • 0030827128 scopus 로고    scopus 로고
    • A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
    • Hinderlich S, Stasche R, Zeitler R, Reutter W. A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. J Biol Chem 1997;272(39):24313-24318.
    • (1997) J Biol Chem , vol.272 , Issue.39 , pp. 24313-24318
    • Hinderlich, S.1    Stasche, R.2    Zeitler, R.3    Reutter, W.4
  • 9
    • 34948865783 scopus 로고    scopus 로고
    • Sialic acid utilization by bacterial pathogens
    • Severi E, Hood DW, Thomas GH. Sialic acid utilization by bacterial pathogens. Microbiology 2007;153(Pt 9):2817-2822.
    • (2007) Microbiology , vol.153 , Issue.PART 9 , pp. 2817-2822
    • Severi, E.1    Hood, D.W.2    Thomas, G.H.3
  • 10
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • Karlsson KA. Microbial recognition of target-cell glycoconjugates. Curr Opin Struct Biol 1995;5(5):622-635.
    • (1995) Curr Opin Struct Biol , vol.5 , Issue.5 , pp. 622-635
    • Karlsson, K.A.1
  • 11
    • 84902144929 scopus 로고    scopus 로고
    • UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE): a master regulator of sialic acid synthesis
    • Epub Jul 11.
    • Hinderlich S, Weidemann W, Yardeni T, Horstkorte R, Huizing M. UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE): a master regulator of sialic acid synthesis. Top Curr Chem Epub 2013 Jul 11.
    • (2013) Top Curr Chem
    • Hinderlich, S.1    Weidemann, W.2    Yardeni, T.3    Horstkorte, R.4    Huizing, M.5
  • 13
    • 0019489031 scopus 로고
    • Metastatic potential is positively correlated with cell surface sialylation of cultured murine tumor cell lines
    • Yogeeswaran G, Salk PL. Metastatic potential is positively correlated with cell surface sialylation of cultured murine tumor cell lines. Science 1981;212(4502):1514-1516.
    • (1981) Science , vol.212 , Issue.4502 , pp. 1514-1516
    • Yogeeswaran, G.1    Salk, P.L.2
  • 14
    • 70449359887 scopus 로고    scopus 로고
    • Crystal structure of the N-acetylmannosamine kinase domain of GNE
    • Tong Y, Tempel W, Nedyalkova L, Mackenzie F, Park HW. Crystal structure of the N-acetylmannosamine kinase domain of GNE. PLoS One 2009;4(10):e7165.
    • (2009) PLoS One , vol.4 , Issue.10
    • Tong, Y.1    Tempel, W.2    Nedyalkova, L.3    Mackenzie, F.4    Park, H.W.5
  • 15
    • 0034642186 scopus 로고    scopus 로고
    • The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
    • Campbell RE, Mosimann SC, Tanner ME, Strynadka NC. The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases. Biochemistry 2000;39(49):14993-15001.
    • (2000) Biochemistry , vol.39 , Issue.49 , pp. 14993-15001
    • Campbell, R.E.1    Mosimann, S.C.2    Tanner, M.E.3    Strynadka, N.C.4
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 1997;276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 2007;63(Pt 1):32-41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , Issue.PART 1 , pp. 32-41
    • McCoy, A.J.1
  • 23
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15(4):305-308.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 25
    • 2942720540 scopus 로고    scopus 로고
    • Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli
    • Samuel J, Tanner ME. Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli. Biochim Biophys Acta 2004;1700(1):85-91.
    • (2004) Biochim Biophys Acta , vol.1700 , Issue.1 , pp. 85-91
    • Samuel, J.1    Tanner, M.E.2
  • 26
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S, Berendsen HJ. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 1998;30(2):144-154.
    • (1998) Proteins , vol.30 , Issue.2 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.