메뉴 건너뛰기




Volumn 346, Issue 4, 2005, Pages 1035-1046

Crystal structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin

Author keywords

Antioxidant; Crystal structure; Mycobacterium tuberculosis; Peroxiredoxin; Redox mechanism

Indexed keywords

PEROXIREDOXIN; PROTEIN AHPE; SODIUM BROMIDE; SULFENIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 13444260861     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.046     Document Type: Article
Times cited : (70)

References (37)
  • 1
    • 0033581124 scopus 로고    scopus 로고
    • Global burden of tuberculosis: Estimated incidence, prevalence and mortality by country
    • C. Dye, S. Scheele, P. Dolin, V. Pathania, and M.C. Raviglione Global burden of tuberculosis: estimated incidence, prevalence and mortality by country J. Am. Med. Assoc. 282 1999 677 686
    • (1999) J. Am. Med. Assoc. , vol.282 , pp. 677-686
    • Dye, C.1    Scheele, S.2    Dolin, P.3    Pathania, V.4    Raviglione, M.C.5
  • 2
    • 0031939281 scopus 로고    scopus 로고
    • Mechanisms of latency in Mycobacterium tuberculosis
    • N.M. Parrish, J.D. Dick, and W.R. Bishai Mechanisms of latency in Mycobacterium tuberculosis Trends Microbiol. 6 1998 107 112
    • (1998) Trends Microbiol. , vol.6 , pp. 107-112
    • Parrish, N.M.1    Dick, J.D.2    Bishai, W.R.3
  • 3
    • 0342794213 scopus 로고    scopus 로고
    • Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase
    • J.D. McKinney, K. Honer zu Bentrup, E.J. Munoz-Elias, A. Miczak, B. Chen, and W.T. Chan Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase Nature 406 2000 735 738
    • (2000) Nature , vol.406 , pp. 735-738
    • McKinney, J.D.1    Honer Zu Bentrup, K.2    Munoz-Elias, E.J.3    Miczak, A.4    Chen, B.5    Chan, W.T.6
  • 4
    • 0032944213 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro
    • C. Manca, S. Paul, C.E. Barry, V.H. Freedman, and G. Kaplan Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro Infect. Immun. 67 1999 74 79
    • (1999) Infect. Immun. , vol.67 , pp. 74-79
    • Manca, C.1    Paul, S.2    Barry, C.E.3    Freedman, V.H.4    Kaplan, G.5
  • 6
  • 8
    • 0037197672 scopus 로고    scopus 로고
    • Dimers to doughnuts: Redox-sensitive oligomerization of 2-Cysteine peroxiredoxins
    • Z.A. Wood, L.B. Poole, R.R. Hantgan, and P.A. Karplus Dimers to doughnuts: redox-sensitive oligomerization of 2-Cysteine peroxiredoxins Biochemistry 41 2002 5493 5504
    • (2002) Biochemistry , vol.41 , pp. 5493-5504
    • Wood, Z.A.1    Poole, L.B.2    Hantgan, R.R.3    Karplus, P.A.4
  • 9
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • S.T. Cole, R. Brosch, J. Parkhill, T. Garnier, C. Churcher, and D. Harris Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence Nature 393 1998 537 544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 10
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • R. Bryk, C.D. Lima, H. Erdjument-Bromage, P. Tempst, and C. Nathan Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein Science 295 2002 1073 1077
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 11
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
    • J. Fujii, and Y. Ikeda Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein Redox Rep. 7 2002 123 130
    • (2002) Redox Rep. , vol.7 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 13
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • R. Bryk, P. Griffin, and C. Nathan Peroxynitrite reductase activity of bacterial peroxiredoxins Nature 407 2000 211 215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 14
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase
    • H.R. Ellis, and L.B. Poole Novel application of 7-chloro-4-nitrobenzo-2- oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase Biochemistry 36 1997 15013 15018
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 15
  • 16
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • W.A. Hendrickson Determination of macromolecular structures from anomalous diffraction of synchrotron radiation Science 254 1991 51 58
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 17
  • 18
    • 0034697984 scopus 로고    scopus 로고
    • The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
    • M.S. Alphey, C.S. Bond, E. Tetaud, A.H. Fairlamb, and W.N. Hunter The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins J. Mol. Biol. 300 2000 903 916
    • (2000) J. Mol. Biol. , vol.300 , pp. 903-916
    • Alphey, M.S.1    Bond, C.S.2    Tetaud, E.3    Fairlamb, A.H.4    Hunter, W.N.5
  • 19
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • S. Hirotsu, Y. Abe, K. Okada, N. Nagahara, H. Hori, T. Nishino, and T. Hakoshima Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product Proc. Natl Acad. Sci. USA 96 1999 12333 12338
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12333-12338
    • Hirotsu, S.1    Abe, Y.2    Okada, K.3    Nagahara, N.4    Hori, H.5    Nishino, T.6    Hakoshima, T.7
  • 20
    • 0038532262 scopus 로고    scopus 로고
    • The tetrameric structure of Haemophilus influenzae hybrid Prx5 reveals interactions between electron donor and acceptor proteins
    • S.J. Kim, J.R. Woo, Y.S. Hwang, D.G. Jeong, D.H. Shin, K. Kim, and S.E. Ryu The tetrameric structure of Haemophilus influenzae hybrid Prx5 reveals interactions between electron donor and acceptor proteins J. Biol. Chem. 278 2003 10790 10798
    • (2003) J. Biol. Chem. , vol.278 , pp. 10790-10798
    • Kim, S.J.1    Woo, J.R.2    Hwang, Y.S.3    Jeong, D.G.4    Shin, D.H.5    Kim, K.6    Ryu, S.E.7
  • 21
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution
    • J.-P. Declercq, C. Evrard, A. Clippe, D.V. Stricht, A. Bernard, and B. Knoops Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution J. Mol. Biol. 311 2001 751 759
    • (2001) J. Mol. Biol. , vol.311 , pp. 751-759
    • Declercq, J.-P.1    Evrard, C.2    Clippe, A.3    Stricht, D.V.4    Bernard, A.5    Knoops, B.6
  • 23
    • 0001084370 scopus 로고
    • Cylinder protein isolated from rat liver mitochondria
    • H. Kato, M. Asanoi, T. Nakazawa, and K. Murayama Cylinder protein isolated from rat liver mitochondria Zool. Sci. 2 1985 485 490
    • (1985) Zool. Sci. , vol.2 , pp. 485-490
    • Kato, H.1    Asanoi, M.2    Nakazawa, T.3    Murayama, K.4
  • 24
    • 0035425780 scopus 로고    scopus 로고
    • Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite
    • I.V. Peshenko, and H. Shichi Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite Free Radical Biol. Med. 31 2001 292 303
    • (2001) Free Radical Biol. Med. , vol.31 , pp. 292-303
    • Peshenko, I.V.1    Shichi, H.2
  • 26
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • W.A. Hendrickson, J.R. Horton, and D.M. LeMaster Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure EMBO J. 9 1990 1665 1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0031058188 scopus 로고    scopus 로고
    • Heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de La Fortelle, and G. Bricogne Heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 30
    • 0033229974 scopus 로고    scopus 로고
    • Reciprocal-space solvent flattening
    • T.C. Terwilliger Reciprocal-space solvent flattening Acta Crystallog. sect. D 55 1999 1863 1871
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 1863-1871
    • Terwilliger, T.C.1
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brunger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 37
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.