메뉴 건너뛰기




Volumn 57, Issue 4, 2004, Pages 878-882

Structural genomics of Pyrococcus furiosus: X-ray crystallography reveals 3D domain swapping in rubrerythrin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; RUBRERYTHRIN; UNCLASSIFIED DRUG;

EID: 10344250940     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20280     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0024281294 scopus 로고
    • Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster
    • Legall J, Prickril BC, Moura I, Xavier AV, Moura JJG, Huynh BH. Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster. Biochemistry 1988;27:1636-1642.
    • (1988) Biochemistry , vol.27 , pp. 1636-1642
    • Legall, J.1    Prickril, B.C.2    Moura, I.3    Xavier, A.V.4    Moura, J.J.G.5    Huynh, B.H.6
  • 2
    • 0029949340 scopus 로고    scopus 로고
    • The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination ofrubredoxin-like FeS4 and ferritin-like diiron domains
    • deMare F, Kurtz DM, Nordlund P. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination ofrubredoxin-like FeS4 and ferritin-like diiron domains. Nat Struct Biol 1996;3:539-546.
    • (1996) Nat Struct Biol , vol.3 , pp. 539-546
    • DeMare, F.1    Kurtz, D.M.2    Nordlund, P.3
  • 3
    • 0024996440 scopus 로고
    • Purification and characterization of 2 proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris rubrerythrin and a new, highly-active, enzyme
    • Liu MY, Legall J. Purification and characterization of 2 proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris rubrerythrin and a new, highly-active, enzyme. Biochem Biophys Res Commun 1990;171:313-318.
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 313-318
    • Liu, M.Y.1    Legall, J.2
  • 4
    • 0027337927 scopus 로고
    • Spectroscopic characterization of Fe-57-reconstituted rubrerythrin, a nonheme iron protein with structural analogies to ribonucleotide reductase
    • Ravi N, Prickril BC, Kurtz DM, Huynh BH. Spectroscopic characterization of Fe-57-reconstituted rubrerythrin, a nonheme iron protein with structural analogies to ribonucleotide reductase. Biochemistry 1993;32:8487-8491.
    • (1993) Biochemistry , vol.32 , pp. 8487-8491
    • Ravi, N.1    Prickril, B.C.2    Kurtz, D.M.3    Huynh, B.H.4
  • 5
    • 0033624219 scopus 로고    scopus 로고
    • The 1.9 angstrom crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: Some surprising results
    • Sieker LC, Holmes M, Le Trong I, Turley S, Liu MY, LeGall J, Stenkamp RE. The 1.9 angstrom crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: some surprising results. J Biol Inorg Chem 2000;5:505-513.
    • (2000) J Biol Inorg Chem , vol.5 , pp. 505-513
    • Sieker, L.C.1    Holmes, M.2    Le Trong, I.3    Turley, S.4    Liu, M.Y.5    LeGall, J.6    Stenkamp, R.E.7
  • 6
    • 0002599331 scopus 로고    scopus 로고
    • Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin
    • Bonomi F, Kurtz DM, Cui XY. Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin. J Biol Inorg Chem 1996;1:67-72.
    • (1996) J Biol Inorg Chem , vol.1 , pp. 67-72
    • Bonomi, F.1    Kurtz, D.M.2    Cui, X.Y.3
  • 7
    • 0035476428 scopus 로고    scopus 로고
    • A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
    • Coulter ED, Kurtz DM. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch Biochem Biophys 2001;394:76-86.
    • (2001) Arch Biochem Biophys , vol.394 , pp. 76-86
    • Coulter, E.D.1    Kurtz, D.M.2
  • 10
    • 0031982010 scopus 로고    scopus 로고
    • A hydrogen peroxide resistant mutant of Spirillum volutans has NADH peroxidase activity but no increased oxygen tolerance
    • Alban PS, Krieg NR. A hydrogen peroxide resistant mutant of Spirillum volutans has NADH peroxidase activity but no increased oxygen tolerance. Can J Microbiol 1998;44:87-91.
    • (1998) Can J Microbiol , vol.44 , pp. 87-91
    • Alban, P.S.1    Krieg, N.R.2
  • 11
    • 9244263012 scopus 로고    scopus 로고
    • Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase
    • In press
    • Weinberg MV, Jenney FE, Jr., Cui X, Adams MWW. Rubrerythrin from the hyperthermophilic archaeon Pyrococcus furiosus is a rubredoxin-dependent, iron-containing peroxidase. J Bacteriol 2004. In press.
    • (2004) J Bacteriol
    • Weinberg, M.V.1    Jenney Jr., F.E.2    Cui, X.3    Adams, M.W.W.4
  • 12
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney FE, Verhagen MFJM, Cui XY, Adams MWW. Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 1999;286:306-309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney, F.E.1    Verhagen, M.F.J.M.2    Cui, X.Y.3    Adams, M.W.W.4
  • 15
    • 0027968068 scopus 로고
    • Clustal-W - Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 16
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks. Computer methods for macromolecular sequence analysis
    • Rost B. PHD: predicting one-dimensional protein structure by profile-based neural networks. Computer Methods for Macromolecular Sequence Analysis. Methods Enzymol 1996;266:525-539.
    • (1996) Methods Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 17
    • 0030565879 scopus 로고    scopus 로고
    • A comparison of microbatch and vapour diffusion for initial screening of crystallization conditions
    • Baldock P, Mills V, Stewart PS. A comparison of microbatch and vapour diffusion for initial screening of crystallization conditions. J Cryst Growth 1996;168:170-174.
    • (1996) J Cryst Growth , vol.168 , pp. 170-174
    • Baldock, P.1    Mills, V.2    Stewart, P.S.3
  • 18
    • 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. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger TC. Automated structure solution, density modification and model building. Acta Crystallogr D Biol Crystallogr 2002;58:1937-1940.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 21
    • 0032790081 scopus 로고    scopus 로고
    • XtalView Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE. XtalView Xfit - a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 1999;125:156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 24
  • 27
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y, Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci 2002;11:1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 28
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: A sketchpad for protein structure topology cartoons
    • Bond CS. TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 2003;19:311-312.
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1
  • 29
    • 0141954187 scopus 로고    scopus 로고
    • Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping
    • Fushinobu S, Shoun H, Wakagi T. Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping. Biochemistry 2003;42:11707-11715.
    • (2003) Biochemistry , vol.42 , pp. 11707-11715
    • Fushinobu, S.1    Shoun, H.2    Wakagi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.