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Volumn 354, Issue 1, 2005, Pages 107-120

Crystal structure of a bacterial class 2 histone deacetylase homologue

Author keywords

Amidohydrolase; Histone deacetylase; SAHA; X ray crystallography; Zinc ion

Indexed keywords

ACETIC ACID; ACETIC ACID DERIVATIVE; BACTERIAL ENZYME; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE; VORINOSTAT; ZINC ION;

EID: 27344457467     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.09.065     Document Type: Article
Times cited : (149)

References (55)
  • 1
    • 0031434997 scopus 로고    scopus 로고
    • The origin and utility of histone deacetylases
    • S. Khochbin, and A.P. Wolffe The origin and utility of histone deacetylases FEBS Letters 419 1997 157 160
    • (1997) FEBS Letters , vol.419 , pp. 157-160
    • Khochbin, S.1    Wolffe, A.P.2
  • 2
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • D.D. Leipe, and D. Landsman Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily Nucl. Acids Res. 25 1997 3693 3697
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 3
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • I.V. Gregoretti, Y.M. Lee, and H.V. Goodson Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis J. Mol. Biol. 338 2004 17 31
    • (2004) J. Mol. Biol. , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 4
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • M. Grunstein Histone acetylation in chromatin structure and transcription Nature 389 1997 349 352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 6
    • 0036279185 scopus 로고    scopus 로고
    • HDAC's at work: Everyone doing their part
    • C.L. Peterson HDAC's at work: everyone doing their part Mol. Cell 9 2002 921 922
    • (2002) Mol. Cell , vol.9 , pp. 921-922
    • Peterson, C.L.1
  • 7
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • R.J. Lin, L. Nagy, S. Inoue, W. Shao, W.H. Miller Jr, and R.M. Evans Role of the histone deacetylase complex in acute promyelocytic leukaemia Nature 391 1998 811 814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 8
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia
    • F. Grignani, S. De Matteis, C. Nervi, L. Tomassoni, V. Gelmetti, and M. Cioce Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia Nature 391 1998 815 818
    • (1998) Nature , vol.391 , pp. 815-818
    • Grignani, F.1    De Matteis, S.2    Nervi, C.3    Tomassoni, L.4    Gelmetti, V.5    Cioce, M.6
  • 9
    • 0035962644 scopus 로고    scopus 로고
    • Histone deacetylases: A common molecular target for differentiation treatment of acute myeloid leukemias?
    • S. Minucci, C. Nervi, F. Lo Coco, and P.G. Pelicci Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene 20 2001 3110 3115
    • (2001) Oncogene , vol.20 , pp. 3110-3115
    • Minucci, S.1    Nervi, C.2    Lo Coco, F.3    Pelicci, P.G.4
  • 10
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • R.W. Johnstone Histone-deacetylase inhibitors: novel drugs for the treatment of cancer Nature Rev. Drug Discov. 1 2002 287 299
    • (2002) Nature Rev. Drug Discov. , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 11
    • 0037822085 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • R.R. Rosato, and S. Grant Histone deacetylase inhibitors in cancer therapy Cancer Biol. Ther. 2 2003 30 37
    • (2003) Cancer Biol. Ther. , vol.2 , pp. 30-37
    • Rosato, R.R.1    Grant, S.2
  • 12
    • 4544323749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Understanding a new wave of anticancer agents
    • A. Villar-Garea, and M. Esteller Histone deacetylase inhibitors: understanding a new wave of anticancer agents Int. J. Cancer 112 2004 171 178
    • (2004) Int. J. Cancer , vol.112 , pp. 171-178
    • Villar-Garea, A.1    Esteller, M.2
  • 13
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • T. Kouzarides Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19 2000 1176 1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 15
  • 17
    • 11144354218 scopus 로고    scopus 로고
    • A new amidohydrolase from Bordetella or Alcaligenes strain FB188 with similarities to histone deacetylases
    • C. Hildmann, M. Ninkovic, R. Dietrich, D. Wegener, D. Riester, and T. Zimmermann A new amidohydrolase from Bordetella or Alcaligenes strain FB188 with similarities to histone deacetylases J. Bacteriol. 186 2004 2328 2339
    • (2004) J. Bacteriol. , vol.186 , pp. 2328-2339
    • Hildmann, C.1    Ninkovic, M.2    Dietrich, R.3    Wegener, D.4    Riester, D.5    Zimmermann, T.6
  • 18
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • S. Imai, C.M. Armstrong, M. Kaeberlein, and L. Guarente Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase Nature 403 2000 795 800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 20
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • C.M. Grozinger, and S.L. Schreiber Deacetylase enzymes: biological functions and the use of small-molecule inhibitors Chem. Biol. 9 2002 3 16
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 21
    • 0034885934 scopus 로고    scopus 로고
    • Class II histone deacetylases: Structure, function, and regulation
    • N.R. Bertos, A.H. Wang, and X.J. Yang Class II histone deacetylases: structure, function, and regulation Biochem. Cell. Biol. 79 2001 243 252
    • (2001) Biochem. Cell. Biol. , vol.79 , pp. 243-252
    • Bertos, N.R.1    Wang, A.H.2    Yang, X.J.3
  • 23
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • D. Seigneurin-Berny, A. Verdel, S. Curtet, C. Lemercier, J. Garin, S. Rousseaux, and S. Khochbin Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways Mol. Cell. Biol. 21 2001 8035 8044
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 24
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • L. Gao, M.A. Cueto, F. Asselbergs, and P. Atadja Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family J. Biol. Chem. 277 2002 25748 25755
    • (2002) J. Biol. Chem. , vol.277 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 26
    • 0242362600 scopus 로고    scopus 로고
    • Discovery of (aryloxopropenyl)pyrrolyl hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A
    • A. Mai, S. Massa, R. Pezzi, D. Rotili, P. Loidl, and G. Brosch Discovery of (aryloxopropenyl)pyrrolyl hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A J. Med. Chem. 46 2003 4826 4829
    • (2003) J. Med. Chem. , vol.46 , pp. 4826-4829
    • Mai, A.1    Massa, S.2    Pezzi, R.3    Rotili, D.4    Loidl, P.5    Brosch, G.6
  • 27
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin a and cyclic tetrapeptide antibiotics including trapoxin
    • R. Furumai, Y. Komatsu, N. Nishino, S. Khochbin, M. Yoshida, and S. Horinouchi Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin Proc. Natl Acad. Sci. USA 98 2001 87 92
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 28
    • 0037562075 scopus 로고    scopus 로고
    • Chemical genetic modifier screens: Small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation
    • K.M. Koeller, S.J. Haggarty, B.D. Perkins, I. Leykin, J.C. Wong, M.C. Kao, and S.L. Schreiber Chemical genetic modifier screens: small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation Chem. Biol. 10 2003 397 410
    • (2003) Chem. Biol. , vol.10 , pp. 397-410
    • Koeller, K.M.1    Haggarty, S.J.2    Perkins, B.D.3    Leykin, I.4    Wong, J.C.5    Kao, M.C.6    Schreiber, S.L.7
  • 29
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • M.S. Finnin, J.R. Donigian, A. Cohen, V.M. Richon, R.A. Rifkind, and P.A. Marks Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors Nature 401 1999 188 193
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 30
    • 3142562372 scopus 로고    scopus 로고
    • Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases
    • J.R. Somoza, R.J. Skene, B.A. Katz, C. Mol, J.D. Ho, and A.J. Jennings Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases Structure (Camb.) 12 2004 1325 1334
    • (2004) Structure (Camb.) , vol.12 , pp. 1325-1334
    • Somoza, J.R.1    Skene, R.J.2    Katz, B.A.3    Mol, C.4    Ho, J.D.5    Jennings, A.J.6
  • 31
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • A. Vannini, C. Volpari, G. Filocamo, E.C. Casavola, M. Brunetti, and D. Renzoni Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor Proc. Natl Acad. Sci. USA 101 2004 15064 15069
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15064-15069
    • Vannini, A.1    Volpari, C.2    Filocamo, G.3    Casavola, E.C.4    Brunetti, M.5    Renzoni, D.6
  • 32
    • 0036014793 scopus 로고    scopus 로고
    • Metal-ligand geometry relevant to proteins and in proteins: Sodium and potassium
    • M.M. Harding Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium Acta Crystallog. sect. D 58 2002 872 874
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 872-874
    • Harding, M.M.1
  • 33
    • 2942545807 scopus 로고    scopus 로고
    • On the function of the 14 Å long internal cavity of histone deacetylase-like protein: Implications for the design of histone deacetylase inhibitors
    • D.F. Wang, O. Wiest, P. Helquist, H.Y. Lan-Hargest, and N.L. Wiech On the function of the 14 Å long internal cavity of histone deacetylase-like protein: implications for the design of histone deacetylase inhibitors J. Med. Chem. 47 2004 3409 3417
    • (2004) J. Med. Chem. , vol.47 , pp. 3409-3417
    • Wang, D.F.1    Wiest, O.2    Helquist, P.3    Lan-Hargest, H.Y.4    Wiech, N.L.5
  • 34
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • C.S. Craik, S. Roczniak, C. Largman, and W.J. Rutter The catalytic role of the active site aspartic acid in serine proteases Science 237 1987 909 913
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 35
    • 0023161184 scopus 로고
    • The three-dimensional structure of Asn102 mutant of trypsin: Role of Asp102 in serine protease catalysis
    • S. Sprang, T. Standing, R.J. Fletterick, R.M. Stroud, J. Finer-Moore, and N.H. Xuong The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis Science 237 1987 905 909
    • (1987) Science , vol.237 , pp. 905-909
    • Sprang, S.1    Standing, T.2    Fletterick, R.J.3    Stroud, R.M.4    Finer-Moore, J.5    Xuong, N.H.6
  • 36
  • 37
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • C.M. Grozinger, C.A. Hassig, and S.L. Schreiber Three proteins define a class of human histone deacetylases related to yeast Hda1p Proc. Natl Acad. Sci. USA 96 1999 4868 4873
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 38
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • S.J. Haggarty, K.M. Koeller, J.C. Wong, C.M. Grozinger, and S.L. Schreiber Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation Proc. Natl Acad. Sci. USA 100 2003 4389 4394
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 39
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homolog of tubulin?
    • H.P. Erickson FtsZ, a prokaryotic homolog of tubulin? Cell 80 1995 367 370
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 40
    • 0032574810 scopus 로고    scopus 로고
    • Acetylation of Lys-92 enhances signaling by the chemotaxis response regulator protein CheY
    • R. Ramakrishnan, M. Schuster, and R.B. Bourret Acetylation of Lys-92 enhances signaling by the chemotaxis response regulator protein CheY Proc. Natl Acad. Sci. USA 95 1998 4918 4923
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4918-4923
    • Ramakrishnan, R.1    Schuster, M.2    Bourret, R.B.3
  • 41
    • 0033607476 scopus 로고    scopus 로고
    • Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kDa protein
    • K. Reuter, S. Nottrott, P. Fabrizio, R. Lührmann, and R. Ficner Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kDa protein J. Mol. Biol. 294 1999 515 525
    • (1999) J. Mol. Biol. , vol.294 , pp. 515-525
    • Reuter, K.1    Nottrott, S.2    Fabrizio, P.3    Lührmann, R.4    Ficner, R.5
  • 42
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 43
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs
    • T. Pape, and T.R. Schneider HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs J. Appl. Crystallog. 37 2004 843 844
    • (2004) J. Appl. Crystallog. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 45
    • 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
  • 46
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 47
    • 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 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    Kjeldgaard4
  • 49
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • A.T. Brunger Assessment of phase accuracy by cross validation: the free R value. Methods and applications Acta Crystallog. sect. D 49 1993 24 36
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 50
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 51
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallog. 30 1997 1022 1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 52
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • A.W. Schuttelkopf, and D.M. van Aalten PRODRG: a tool for high-throughput crystallography of protein-ligand complexes Acta Crystallog. sect. D 60 2004 1355 1363
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 53
  • 54
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • G.J. Kleywegt Use of non-crystallographic symmetry in protein structure refinement Acta Crystallog. sect. D 52 1996 842 857
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 55
    • 0141849191 scopus 로고    scopus 로고
    • Improved fluorogenic histone deacetylase assay for high-throughput- screening applications
    • D. Wegener, C. Hildmann, D. Riester, and A. Schwienhorst Improved fluorogenic histone deacetylase assay for high-throughput-screening applications Anal. Biochem. 321 2003 202 208
    • (2003) Anal. Biochem. , vol.321 , pp. 202-208
    • Wegener, D.1    Hildmann, C.2    Riester, D.3    Schwienhorst, A.4


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