메뉴 건너뛰기




Volumn 414, Issue 3, 2011, Pages 487-492

Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension

Author keywords

Dihydroorotate dehydrogenase; Electron spin resonance; Membrane association; Site directed spin labeling; Vesicles

Indexed keywords

DIHYDROOROTATE DEHYDROGENASE; QUINONE DERIVATIVE;

EID: 80054890079     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.09.092     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 0031423109 scopus 로고    scopus 로고
    • Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis
    • Bjornberg O., Rowland P., Larsen S., Jensen K.F. Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry 1997, 36:16197-16205.
    • (1997) Biochemistry , vol.36 , pp. 16197-16205
    • Bjornberg, O.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 4
    • 0034122123 scopus 로고    scopus 로고
    • Leflunomide: an immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases
    • Herrmann M.L., Schleyerbach R., Kirschbaum B.J. Leflunomide: an immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases. Immunopharmacology 2000, 47:273-289.
    • (2000) Immunopharmacology , vol.47 , pp. 273-289
    • Herrmann, M.L.1    Schleyerbach, R.2    Kirschbaum, B.J.3
  • 5
    • 33646860532 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of Leishmania major dihydroorotate dehydrogenase, Protein
    • Feliciano P.R., Cordeiro A.T., Costa A.J., Nonato M.C. Cloning, expression, purification, and characterization of Leishmania major dihydroorotate dehydrogenase, Protein. Expression Purif. 2006, 48:98-103.
    • (2006) Expression Purif. , vol.48 , pp. 98-103
    • Feliciano, P.R.1    Cordeiro, A.T.2    Costa, A.J.3    Nonato, M.C.4
  • 6
    • 53749085717 scopus 로고    scopus 로고
    • Structures of trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction
    • Inaoka D.K., Sakamoto K., Shimizu H., Shiba T., Kurisu G., Nara T., Aoki T., Kita K., Harada S. Structures of trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction. Biochemistry 2008, 47:10881-10891.
    • (2008) Biochemistry , vol.47 , pp. 10881-10891
    • Inaoka, D.K.1    Sakamoto, K.2    Shimizu, H.3    Shiba, T.4    Kurisu, G.5    Nara, T.6    Aoki, T.7    Kita, K.8    Harada, S.9
  • 7
    • 0028359494 scopus 로고
    • Different dihydroorotate dehydrogenases in Lactococcus lactis
    • Andersen P.S., Jansen P.J.G., Hammer K. Different dihydroorotate dehydrogenases in Lactococcus lactis. J. Bacteriol. 1994, 176:3975-3982.
    • (1994) J. Bacteriol. , vol.176 , pp. 3975-3982
    • Andersen, P.S.1    Jansen, P.J.G.2    Hammer, K.3
  • 8
    • 0017795563 scopus 로고
    • Dihydroorotate dehydrogenase (Escherichia coli)
    • Karibian D. Dihydroorotate dehydrogenase (Escherichia coli). Methods Enzymol. 1978, 51:58-63.
    • (1978) Methods Enzymol. , vol.51 , pp. 58-63
    • Karibian, D.1
  • 9
    • 0021934210 scopus 로고
    • Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase
    • Larsen J.N., Jensen K.F. Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase. Eur. J. Biochem. 1985, 151:59-65.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 59-65
    • Larsen, J.N.1    Jensen, K.F.2
  • 10
    • 0029793899 scopus 로고    scopus 로고
    • Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified enzyme
    • Knecht W., Bergjohann U., Gonski S., Kirschbaum B., Loffler M. Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified enzyme. Eur. J. Biochem. 1996, 240:292-301.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 292-301
    • Knecht, W.1    Bergjohann, U.2    Gonski, S.3    Kirschbaum, B.4    Loffler, M.5
  • 11
    • 41149141262 scopus 로고    scopus 로고
    • Crystal structure of Trypanosoma cruzi dihydroorotate dehydrogenase from Y strain
    • Pinheiro M.P., Iulek J., Nonato M.C. Crystal structure of Trypanosoma cruzi dihydroorotate dehydrogenase from Y strain. Biochem. Biophys. Res. Commun. 2008, 369:812-817.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 812-817
    • Pinheiro, M.P.1    Iulek, J.2    Nonato, M.C.3
  • 12
    • 0043209013 scopus 로고    scopus 로고
    • Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
    • Norager S., Arent S., Bjornberg O., Ottosen M., Lo Leggio L., Jensen K.F., Larsen S. Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function. J. Biol. Chem. 2003, 278:28812-28822.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28812-28822
    • Norager, S.1    Arent, S.2    Bjornberg, O.3    Ottosen, M.4    Lo Leggio, L.5    Jensen, K.F.6    Larsen, S.7
  • 13
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents
    • Liu S.P., Neidhardt E.A., Grossman T.H., Ocain T., Clardy J. Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Struct. Fold. Des. 2000, 8:25-33.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 25-33
    • Liu, S.P.1    Neidhardt, E.A.2    Grossman, T.H.3    Ocain, T.4    Clardy, J.5
  • 14
    • 33646583490 scopus 로고    scopus 로고
    • Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor
    • Hurt D.E., Widom J., Clardy J. Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62:312-323.
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 312-323
    • Hurt, D.E.1    Widom, J.2    Clardy, J.3
  • 15
    • 0041433824 scopus 로고    scopus 로고
    • E-coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases
    • Norager S., Jensen K.F., Bjornberg O., Larsen S. E-coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure 2002, 10:1211-1223.
    • (2002) Structure , vol.10 , pp. 1211-1223
    • Norager, S.1    Jensen, K.F.2    Bjornberg, O.3    Larsen, S.4
  • 16
    • 1842559337 scopus 로고    scopus 로고
    • Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain
    • Hansen M., Le Nours J., Johansson E., Antal T., Ullrich A., Loffler M., Larsen S. Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain. Protein Sci. 2004, 13:1031-1042.
    • (2004) Protein Sci. , vol.13 , pp. 1031-1042
    • Hansen, M.1    Le Nours, J.2    Johansson, E.3    Antal, T.4    Ullrich, A.5    Loffler, M.6    Larsen, S.7
  • 17
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents
    • Norager S., Jensen K.F., Bj€ornberg O., Larsen S. Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure 2002, 8:25-33.
    • (2002) Structure , vol.8 , pp. 25-33
    • Norager, S.1    Jensen, K.F.2    Bj€ornberg, O.3    Larsen, S.4
  • 18
    • 41149141088 scopus 로고    scopus 로고
    • Defects in vesicle core induced by Escherichia coli dihydroorotate dehydrogenase
    • Couto S.G., Nonato M.C., Costa-Filho A.J. Defects in vesicle core induced by Escherichia coli dihydroorotate dehydrogenase. Biophys. J. 2008, 94:1746-1753.
    • (2008) Biophys. J. , vol.94 , pp. 1746-1753
    • Couto, S.G.1    Nonato, M.C.2    Costa-Filho, A.J.3
  • 19
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci G.E., Cafiso D.S. Recent advances and applications of site-directed spin labeling. Curr. Opin. Struct. Biol. 2006, 16:644-653.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 20
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2 Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach C., Flitsch S.L., Khorana H.G., Hubbell W.L. Structural studies on transmembrane proteins. 2 Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry 1989, 28:7806-7812.
    • (1989) Biochemistry , vol.28 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.G.3    Hubbell, W.L.4
  • 21
    • 0036606899 scopus 로고    scopus 로고
    • A new spin on protein dynamics
    • Columbus L., Hubbell W.L. A new spin on protein dynamics. TIBS 2002, 27:288-295.
    • (2002) TIBS , vol.27 , pp. 288-295
    • Columbus, L.1    Hubbell, W.L.2
  • 22
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell W.L., Cafiso D.S., Altenbach C. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 2000, 7:735-739.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 24
    • 0039021706 scopus 로고    scopus 로고
    • The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis
    • Bjornberg O., Gruner A.C., Roepstorff P., Jensen K.F. The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry 1999, 38:2899-2908.
    • (1999) Biochemistry , vol.38 , pp. 2899-2908
    • Bjornberg, O.1    Gruner, A.C.2    Roepstorff, P.3    Jensen, K.F.4
  • 25
    • 0001867405 scopus 로고
    • Calculating slow motional magnetic resonance spectra: a user's guide
    • Plenum Publishing, New York, L.J. Berliner, J. Reuben (Eds.)
    • Schneider D.J., Freed J.H. Calculating slow motional magnetic resonance spectra: a user's guide. Biological Magnetic Resonance 1989, 1-76. Plenum Publishing, New York. L.J. Berliner, J. Reuben (Eds.).
    • (1989) Biological Magnetic Resonance , pp. 1-76
    • Schneider, D.J.1    Freed, J.H.2
  • 26
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm
    • Budil D.E., Lee S., Saxena S., Freed J.H. Nonlinear-least squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. J. Magn. Reson. 1996, A120:155-189.
    • (1996) J. Magn. Reson. , vol.A120 , pp. 155-189
    • Budil, D.E.1    Lee, S.2    Saxena, S.3    Freed, J.H.4
  • 27
    • 2942527068 scopus 로고    scopus 로고
    • Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA
    • Columbus L., Hubbell W.L. Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA. Biochemistry 2004, 43:7273-7287.
    • (2004) Biochemistry , vol.43 , pp. 7273-7287
    • Columbus, L.1    Hubbell, W.L.2
  • 28
    • 17844377971 scopus 로고    scopus 로고
    • EPR studies of chlorocatechol 1 2-dioxygenase: Evidences of iron reduction during catalysis and of the binding of amphipatic molecules
    • Citadini A.P.S., Pinto A.P.A., Araújo A.P.U., Nascimento O.R., Costa-Filho A.J. EPR studies of chlorocatechol 1 2-dioxygenase: Evidences of iron reduction during catalysis and of the binding of amphipatic molecules. Biophys. J. 2005, 88:3502-3508.
    • (2005) Biophys. J. , vol.88 , pp. 3502-3508
    • Citadini, A.P.S.1    Pinto, A.P.A.2    Araújo, A.P.U.3    Nascimento, O.R.4    Costa-Filho, A.J.5
  • 29
    • 0041343028 scopus 로고    scopus 로고
    • Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells
    • Ge M.T., Gidwani A., Brown H.A., Holowka D., Baird B., Freed J.F. Ordered and disordered phases coexist in plasma membrane vesicles of RBL-2H3 mast cells. Biophys. J. 2003, 85:1278-1288.
    • (2003) Biophys. J. , vol.85 , pp. 1278-1288
    • Ge, M.T.1    Gidwani, A.2    Brown, H.A.3    Holowka, D.4    Baird, B.5    Freed, J.F.6
  • 31
    • 34250375257 scopus 로고    scopus 로고
    • Detergent-dependent kinetics of truncated plasmodium falciparum dihydroorotate dehydrogenase
    • Malmquist N.A., Baldwin J., Phillips M.A. Detergent-dependent kinetics of truncated plasmodium falciparum dihydroorotate dehydrogenase. J. Biol. Chem. 2007, 282:12678-12686.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12678-12686
    • Malmquist, N.A.1    Baldwin, J.2    Phillips, M.A.3
  • 32
    • 0041154173 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in t4 lysozyme: effect of side chain structure
    • Mchaourab H.S., Kálai T., Hideg K., Hubbell W.L. Motion of spin-labeled side chains in t4 lysozyme: effect of side chain structure. Biochemistry 1999, 38:2947-2955.
    • (1999) Biochemistry , vol.38 , pp. 2947-2955
    • Mchaourab, H.S.1    Kálai, T.2    Hideg, K.3    Hubbell, W.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.