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Volumn 467, Issue 1, 2015, Pages 103-113

Structural basis of cofactor-mediated stabilization and substrate recognition of the α-tubulin acetyltransferase αTAT1

Author keywords

Coenzyme A; Crystal structure; Mechanosensory (MEC) 17; Substrate recognition; tubulin acetyltransferase 1 ( TAT1)

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; ALANINE; ALPHA TUBULIN; ALPHA TUBULIN ACETYLTRANSFERASE 1; ARGININE; COENZYME A; HISTONE ACETYLTRANSFERASE; UNCLASSIFIED DRUG; ALPHA-TUBULIN ACETYLASE; HYBRID PROTEIN; MUTANT PROTEIN; PEPTIDE FRAGMENT; SERINE; TUBA1A PROTEIN, HUMAN; TUBULIN;

EID: 84929939021     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141193     Document Type: Article
Times cited : (6)

References (63)
  • 1
    • 0037452091 scopus 로고    scopus 로고
    • Molecular motors
    • CrossRef PubMed
    • Schliwa, M. and Woehlke, G. (2003) Molecular motors. Nature 422, 759-765 CrossRef PubMed
    • (2003) Nature , vol.422 , pp. 759-765
    • Schliwa, M.1    Woehlke, G.2
  • 2
    • 54149116728 scopus 로고    scopus 로고
    • Swimming with protists: Perception, motility and flagellum assembly
    • CrossRef PubMed
    • Ginger, M.L., Portman, N. and McKean, P.G. (2008) Swimming with protists: perception, motility and flagellum assembly. Nat. Rev. Microbiol. 6, 838-850 CrossRef PubMed
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 838-850
    • Ginger, M.L.1    Portman, N.2    McKean, P.G.3
  • 3
    • 84871530214 scopus 로고    scopus 로고
    • Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore
    • CrossRef PubMed
    • Foley, E.A. and Kapoor, T.M. (2013) Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore. Nat. Rev. Mol. Cell Biol. 14, 25-37 CrossRef PubMed
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 25-37
    • Foley, E.A.1    Kapoor, T.M.2
  • 4
    • 84863774430 scopus 로고    scopus 로고
    • The chemical complexity of cellular microtubules: Tubulin post-translational modification enzymes and their roles in tuning microtubule functions
    • CrossRef PubMed
    • Garnham, C.P. and Roll-Mecak, A. (2012) The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions. Cytoskeleton 69, 442-463 CrossRef PubMed
    • (2012) Cytoskeleton , vol.69 , pp. 442-463
    • Garnham, C.P.1    Roll-Mecak, A.2
  • 5
    • 34548830425 scopus 로고    scopus 로고
    • The tubulin code
    • CrossRef
    • Verhey, K.J. and Gaertig, J. (2007) The tubulin code. Cell Cycle 17, 2152-2160 CrossRef
    • (2007) Cell Cycle , vol.17 , pp. 2152-2160
    • Verhey, K.J.1    Gaertig, J.2
  • 6
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • CrossRef PubMed
    • Janke, C. and Bulinski, J.C. (2011) Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat. Rev. Mol. Cell Biol. 12, 773-786 CrossRef PubMed
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 8
    • 78650731392 scopus 로고    scopus 로고
    • The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • CrossRef PubMed
    • Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. (2010) The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. U.S.A. 107, 21517-21522 CrossRef PubMed
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 10
    • 84880066266 scopus 로고    scopus 로고
    • Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion
    • CrossRef PubMed
    • Kim, G.W., Li, L., Gorbani, M., You, L. and Yang, X.J. (2013) Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion. J. Biol. Chem. 288, 20334-20350 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 20334-20350
    • Kim, G.W.1    Li, L.2    Gorbani, M.3    You, L.4    Yang, X.J.5
  • 12
    • 84862658847 scopus 로고    scopus 로고
    • Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules
    • CrossRef PubMed
    • Cueva, J.G., Hsin, J., Huang, K.C. and Goodman, M.B. (2012) Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules. Curr. Biol. 22, 1066-1074 CrossRef PubMed
    • (2012) Curr. Biol. , vol.22 , pp. 1066-1074
    • Cueva, J.G.1    Hsin, J.2    Huang, K.C.3    Goodman, M.B.4
  • 13
    • 0033877252 scopus 로고    scopus 로고
    • GCN5-related N-acetyltransferases: A structural overview
    • CrossRef PubMed
    • Dyda, F., Klein, D.C. and Hickman, A.B. (2000) GCN5-related N-acetyltransferases: a structural overview. Annu. Rev. Biophys. Biomol. Struct. 29, 81-103 CrossRef PubMed
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 81-103
    • Dyda, F.1    Klein, D.C.2    Hickman, A.B.3
  • 15
    • 84886599617 scopus 로고    scopus 로고
    • Structure and mechanism of non-histone protein acetyltransferase enzymes
    • CrossRef PubMed
    • Friedmann, D.R. and Marmorstein, R. (2013) Structure and mechanism of non-histone protein acetyltransferase enzymes. FEBS J. 280, 5570-5581 CrossRef PubMed
    • (2013) FEBS J. , vol.280 , pp. 5570-5581
    • Friedmann, D.R.1    Marmorstein, R.2
  • 16
    • 84870316474 scopus 로고    scopus 로고
    • Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA
    • CrossRef PubMed
    • Taschner, M., Vetter, M. and Lorentzen, E. (2012) Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. U.S.A. 109, 19649-19654 CrossRef PubMed
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19649-19654
    • Taschner, M.1    Vetter, M.2    Lorentzen, E.3
  • 17
    • 84870342617 scopus 로고    scopus 로고
    • Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation
    • CrossRef PubMed
    • Friedmann, D.R., Aguilar, A., Fan, J., Nachury, M.V. and Marmorstein, R. (2012) Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. U.S.A. 109, 19655-19660 CrossRef PubMed
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19655-19660
    • Friedmann, D.R.1    Aguilar, A.2    Fan, J.3    Nachury, M.V.4    Marmorstein, R.5
  • 18
    • 84871287765 scopus 로고    scopus 로고
    • Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus
    • CrossRef PubMed
    • Kormendi, V., Szyk, A., Piszczek, G. and Roll-Mecak, A. (2012) Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus. J. Biol. Chem. 287, 41569-41575 CrossRef PubMed
    • (2012) J. Biol. Chem. , vol.287 , pp. 41569-41575
    • Kormendi, V.1    Szyk, A.2    Piszczek, G.3    Roll-Mecak, A.4
  • 19
    • 84870582570 scopus 로고    scopus 로고
    • Molecular basis of the acetyltransferase activity of MEC-17 towards α-tubulin
    • CrossRef PubMed
    • Li, W., Zhong, C., Li, L., Sun, B., Wang, W., Xu, S., Zhang, T., Wang, C., Bao, L. and Ding, J. (2012) Molecular basis of the acetyltransferase activity of MEC-17 towards α-tubulin. Cell Res. 22, 1707-1711 CrossRef PubMed
    • (2012) Cell Res. , vol.22 , pp. 1707-1711
    • Li, W.1    Zhong, C.2    Li, L.3    Sun, B.4    Wang, W.5    Xu, S.6    Zhang, T.7    Wang, C.8    Bao, L.9    Ding, J.10
  • 20
    • 84903136526 scopus 로고    scopus 로고
    • Structural and functional characterization of the α-tubulin acetyltransferase MEC-17
    • CrossRef PubMed
    • Davenport, A.M., Collins, L.N., Chiu, H., Minor, P.J., Sternberg, P.W. and Hoelz, A. (2014) Structural and functional characterization of the α-tubulin acetyltransferase MEC-17. J. Mol. Biol. 426, 2605-2616 CrossRef PubMed
    • (2014) J. Mol. Biol. , vol.426 , pp. 2605-2616
    • Davenport, A.M.1    Collins, L.N.2    Chiu, H.3    Minor, P.J.4    Sternberg, P.W.5    Hoelz, A.6
  • 22
    • 82755163576 scopus 로고    scopus 로고
    • Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN)
    • CrossRef PubMed
    • Yuzawa, S., Kamakura, S., Iwakiri, Y., Hayase, J. and Sumimoto, H. (2011) Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN). Proc. Natl. Acad. Sci. U.S.A. 108, 19210-19215 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19210-19215
    • Yuzawa, S.1    Kamakura, S.2    Iwakiri, Y.3    Hayase, J.4    Sumimoto, H.5
  • 23
    • 34447531743 scopus 로고    scopus 로고
    • Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor
    • CrossRef PubMed
    • Yuzawa, S., Opatowsky, Y., Zhang, Z., Mandiyan, V., Lax, I. and Schlessinger, J. (2007) Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor. Cell 130, 323-334 CrossRef PubMed
    • (2007) Cell , vol.130 , pp. 323-334
    • Yuzawa, S.1    Opatowsky, Y.2    Zhang, Z.3    Mandiyan, V.4    Lax, I.5    Schlessinger, J.6
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • CrossRef
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 CrossRef
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • CrossRef PubMed
    • Sheldrick, G.M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485 CrossRef PubMed
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 26
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for macromolecular phasing with SHELX programs
    • CrossRef
    • Pape, T. and Schneider, T.R. (2004) HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J. Appl. Crystallogr 37, 843-844 CrossRef
    • (2004) J. Appl. Crystallogr , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 32
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • CrossRef PubMed
    • Hasegawa, H. and Holm, L. (2009) Advances and pitfalls of protein structural alignment. Curr. Opin. Struct. Biol. 19, 341-348 CrossRef PubMed
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 33
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • CrossRef PubMed
    • Krissinel, E. and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 CrossRef PubMed
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 84881546973 scopus 로고    scopus 로고
    • The cell polarity protein mInsc regulates neutrophil chemotaxis via a noncanonical G protein signaling pathway
    • CrossRef PubMed
    • Kamakura, S., Nomura, M., Hayase, J., Iwakiri, Y., Nishikimi, A., Takayanagi, R., Fukui, Y. and Sumimoto, H. (2013) The cell polarity protein mInsc regulates neutrophil chemotaxis via a noncanonical G protein signaling pathway. Dev. Cell 26, 292-302 CrossRef PubMed
    • (2013) Dev. Cell , vol.26 , pp. 292-302
    • Kamakura, S.1    Nomura, M.2    Hayase, J.3    Iwakiri, Y.4    Nishikimi, A.5    Takayanagi, R.6    Fukui, Y.7    Sumimoto, H.8
  • 35
    • 84878985768 scopus 로고    scopus 로고
    • Ubiquitination of the heterotrimeric G protein α subunits Gαi2 and Gαq is prevented by the guanine nucleotide exchange factor Ric-8A
    • CrossRef PubMed
    • Chishiki, K., Kamakura, S., Yuzawa, S., Hayase, J. and Sumimoto, H. (2013) Ubiquitination of the heterotrimeric G protein α subunits Gαi2 and Gαq is prevented by the guanine nucleotide exchange factor Ric-8A. Biochem. Biophys. Res. Commun. 435, 414-419 CrossRef PubMed
    • (2013) Biochem. Biophys. Res. Commun. , vol.435 , pp. 414-419
    • Chishiki, K.1    Kamakura, S.2    Yuzawa, S.3    Hayase, J.4    Sumimoto, H.5
  • 36
    • 0023664065 scopus 로고
    • Regulation of pantothenate kinase by coenzyme A and its thioesters
    • PubMed
    • Vallari, D.S., Jackowski, S. and Rock, C.O. (1987) Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 262, 2468-2471 PubMed
    • (1987) J. Biol. Chem. , vol.262 , pp. 2468-2471
    • Vallari, D.S.1    Jackowski, S.2    Rock, C.O.3
  • 37
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • CrossRef PubMed
    • Rojas, J.R., Trievel, R.C., Zhou, J., Mo, Y., Li, X., Berger, S.L., Allis, C.D. and Marmorstein, R. (1999) Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401, 93-98 CrossRef PubMed
    • (1999) Nature , vol.401 , pp. 93-98
    • Rojas, J.R.1    Trievel, R.C.2    Zhou, J.3    Mo, Y.4    Li, X.5    Berger, S.L.6    Allis, C.D.7    Marmorstein, R.8
  • 38
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily
    • CrossRef PubMed
    • Angus-Hill, M.L., Dutnall, R.N., Tafrov, S.T., Sternglanz, R. and Ramakrishnan, V. (1999) Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily. J. Mol. Biol. 294, 1311-1325 CrossRef PubMed
    • (1999) J. Mol. Biol. , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 39
    • 20444445924 scopus 로고    scopus 로고
    • A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium
    • CrossRef PubMed
    • Vetting, M.W., de Carvalho, L.P., Roderick, S.L. and Blanchard, J.S. (2005) A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium. J. Biol. Chem. 280, 22108-22114 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 22108-22114
    • Vetting, M.W.1    De Carvalho, L.P.2    Roderick, S.L.3    Blanchard, J.S.4
  • 40
    • 33144472475 scopus 로고    scopus 로고
    • Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target
    • CrossRef PubMed
    • Bewley, M.C., Graziano, V., Jiang, J., Matz, E., Studier, F.W., Pegg, A.E., Coleman, C.S. and Flanagan, J.M. (2006) Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Proc. Natl. Acad. Sci. U.S.A. 103, 2063-2068 CrossRef PubMed
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2063-2068
    • Bewley, M.C.1    Graziano, V.2    Jiang, J.3    Matz, E.4    Studier, F.W.5    Pegg, A.E.6    Coleman, C.S.7    Flanagan, J.M.8
  • 41
    • 0033010021 scopus 로고    scopus 로고
    • Melatonin biosynthesis: The structure of serotonin N-acetyltransferase at 2.5 Å resolution suggests a catalytic mechanism
    • CrossRef PubMed
    • Hickman, A.B., Klein, D.C. and Dyda, F. (1999) Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 Å resolution suggests a catalytic mechanism. Mol. Cell 3, 23-32 CrossRef PubMed
    • (1999) Mol. Cell , vol.3 , pp. 23-32
    • Hickman, A.B.1    Klein, D.C.2    Dyda, F.3
  • 42
    • 0036707544 scopus 로고    scopus 로고
    • Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates
    • CrossRef PubMed
    • Vetting, M.W., Hegde, S.S., Javid-Majd, F., Blanchard, J.S. and Roderick, S.L. (2002) Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat. Struct. Biol. 9, 653-658 CrossRef PubMed
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 653-658
    • Vetting, M.W.1    Hegde, S.S.2    Javid-Majd, F.3    Blanchard, J.S.4    Roderick, S.L.5
  • 43
    • 0018337607 scopus 로고
    • Assay of citric acid cycle intermediates and related compounds: Update with tissue metabolite levels and intracellular distribution
    • CrossRef PubMed
    • Williamson, J.R. and Corkey, B.E. (1979) Assay of citric acid cycle intermediates and related compounds: update with tissue metabolite levels and intracellular distribution. Methods Enzymol. 55, 200-222 CrossRef PubMed
    • (1979) Methods Enzymol. , vol.55 , pp. 200-222
    • Williamson, J.R.1    Corkey, B.E.2
  • 44
    • 0022458178 scopus 로고
    • Changes in CoA pools in hepatic peroxisomes of the rat under various conditions
    • PubMed
    • Horie, S., Isobe, M. and Suga, T. (1986) Changes in CoA pools in hepatic peroxisomes of the rat under various conditions. J. Biochem. 99, 1345-1352 PubMed
    • (1986) J. Biochem. , vol.99 , pp. 1345-1352
    • Horie, S.1    Isobe, M.2    Suga, T.3
  • 46
    • 84871046431 scopus 로고    scopus 로고
    • Cation-π interaction: Its role and relevance in chemistry, biology, and material science
    • CrossRef PubMed
    • Mahadevi, A.S. and Sastry, G.N. (2013) Cation-π interaction: its role and relevance in chemistry, biology, and material science. Chem. Rev. 113, 2100-2138 CrossRef PubMed
    • (2013) Chem. Rev. , vol.113 , pp. 2100-2138
    • Mahadevi, A.S.1    Sastry, G.N.2
  • 47
    • 0344443398 scopus 로고    scopus 로고
    • Multiple intermolecular interaction modes of positively charged residues with adenine in ATP-binding proteins
    • CrossRef PubMed
    • Mao, L., Wang, Y., Liu, Y. and Hu, X. (2003) Multiple intermolecular interaction modes of positively charged residues with adenine in ATP-binding proteins. J. Am. Chem. Soc. 125, 14216-14217 CrossRef PubMed
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14216-14217
    • Mao, L.1    Wang, Y.2    Liu, Y.3    Hu, X.4
  • 48
    • 80054694313 scopus 로고    scopus 로고
    • Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation
    • CrossRef PubMed
    • Liszczak, G., Arnesen, T. and Marmorstein, R. (2011) Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation. J. Biol. Chem. 286, 37002-37010 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 37002-37010
    • Liszczak, G.1    Arnesen, T.2    Marmorstein, R.3
  • 49
    • 84883342432 scopus 로고    scopus 로고
    • Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog
    • CrossRef PubMed
    • Liszczak, G. and Marmorstein, R. (2013) Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog. Proc. Natl. Acad. Sci. U.S.A. 110, 14652-14657 CrossRef PubMed
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 14652-14657
    • Liszczak, G.1    Marmorstein, R.2
  • 50
    • 84864886655 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1
    • CrossRef PubMed
    • Dorfmueller, H.C., Fang, W., Rao, F.V., Blair, D.E., Attrill, H. and van Aalten, D.M. (2012) Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1. Acta Crystallogr. D Biol. Crystallogr. 68, 1019-1029 CrossRef PubMed
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 1019-1029
    • Dorfmueller, H.C.1    Fang, W.2    Rao, F.V.3    Blair, D.E.4    Attrill, H.5    Van Aalten, D.M.6
  • 51
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • CrossRef PubMed
    • Liu, X, Wang, L., Zhao, K., Thompson, P.R., Hwang, Y., Marmorstein, R. and Cole, P.A. (2008) The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature 451, 846-850 CrossRef PubMed
    • (2008) Nature , vol.451 , pp. 846-850
    • Liu, X.1    Wang, L.2    Zhao, K.3    Thompson, P.R.4    Hwang, Y.5    Marmorstein, R.6    Cole, P.A.7
  • 52
    • 84901953490 scopus 로고    scopus 로고
    • Structure of the p300 histone acetyltransferase bound to acetyl-coenzyme A and its analogues
    • CrossRef PubMed
    • Maksimoska, J., Segura-Peña, D., Cole, P.A. and Marmorstein, R. (2014) Structure of the p300 histone acetyltransferase bound to acetyl-coenzyme A and its analogues. Biochemistry 53, 3415-3422 CrossRef PubMed
    • (2014) Biochemistry , vol.53 , pp. 3415-3422
    • Maksimoska, J.1    Segura-Peña, D.2    Cole, P.A.3    Marmorstein, R.4
  • 53
    • 33747460737 scopus 로고    scopus 로고
    • Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: Construction of a NADH-accepting mutant and its application in rare sugar synthesis
    • CrossRef PubMed
    • Dambe, T.R., Kühn, A.M., Brossette, T., Giffhorn, F. and Scheidig, A.J. (2006) Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis. Biochemistry 45, 10030-10042 CrossRef PubMed
    • (2006) Biochemistry , vol.45 , pp. 10030-10042
    • Dambe, T.R.1    Kühn, A.M.2    Brossette, T.3    Giffhorn, F.4    Scheidig, A.J.5
  • 54
    • 0034254603 scopus 로고    scopus 로고
    • Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: Structural implications for cofactor specificity and affinity
    • PubMed
    • Ahvazi, B., Coulombe, R., Delarge, M., Vedadi, M., Zhang, L., Meighen, E. and Vrielink, A. (2000) Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity. Biochem. J. 349, 853-861 PubMed
    • (2000) Biochem. J. , vol.349 , pp. 853-861
    • Ahvazi, B.1    Coulombe, R.2    Delarge, M.3    Vedadi, M.4    Zhang, L.5    Meighen, E.6    Vrielink, A.7
  • 56
    • 0028773899 scopus 로고
    • Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism
    • CrossRef PubMed
    • Adams, M.J., Ellis, G.H., Gover, S., Naylor, C.E. and Phillips, C. (1994) Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism. Structure 2, 651-668 CrossRef PubMed
    • (1994) Structure , vol.2 , pp. 651-668
    • Adams, M.J.1    Ellis, G.H.2    Gover, S.3    Naylor, C.E.4    Phillips, C.5
  • 57
    • 0347481147 scopus 로고    scopus 로고
    • Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates
    • CrossRef PubMed
    • Poux, A.N. and Marmorstein, R. (2003) Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates. Biochemistry 42, 14366-14374 CrossRef PubMed
    • (2003) Biochemistry , vol.42 , pp. 14366-14374
    • Poux, A.N.1    Marmorstein, R.2
  • 58
    • 84861906071 scopus 로고    scopus 로고
    • Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1
    • CrossRef PubMed
    • Wu, H., Moshkina, N., Min, J., Zeng, H., Joshua, J., Zhou, M.M. and Plotnikov, A.N. (2012) Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1. Proc. Natl. Acad. Sci. U.S.A. 109, 8925-8930 CrossRef PubMed
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 8925-8930
    • Wu, H.1    Moshkina, N.2    Min, J.3    Zeng, H.4    Joshua, J.5    Zhou, M.M.6    Plotnikov, A.N.7
  • 59
    • 0035823497 scopus 로고    scopus 로고
    • Transcriptional coactivator protein p300: Kinetic characterization of its histone acetyltransferase activity
    • CrossRef PubMed
    • Thompson, P.R., Kurooka, H., Nakatani, Y. and Cole, P.A. (2001) Transcriptional coactivator protein p300: kinetic characterization of its histone acetyltransferase activity. J. Biol. Chem. 276, 33721-33729 CrossRef PubMed
    • (2001) J. Biol. Chem. , vol.276 , pp. 33721-33729
    • Thompson, P.R.1    Kurooka, H.2    Nakatani, Y.3    Cole, P.A.4
  • 60
    • 33847655626 scopus 로고    scopus 로고
    • Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex
    • CrossRef PubMed
    • Berndsen, C.E., Selleck, W., McBryant, S.J., Hansen, J.C., Tan, S. and Denu, J.M. (2007) Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex. Biochemistry 46, 2091-2099 CrossRef PubMed
    • (2007) Biochemistry , vol.46 , pp. 2091-2099
    • Berndsen, C.E.1    Selleck, W.2    McBryant, S.J.3    Hansen, J.C.4    Tan, S.5    Denu, J.M.6
  • 61
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • CrossRef PubMed
    • Lee, K.L. and Workman, J.L. (2007) Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol. 8, 284-295 CrossRef PubMed
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 284-295
    • Lee, K.L.1    Workman, J.L.2
  • 62
    • 57049152851 scopus 로고    scopus 로고
    • Catalysis and substrate selection by histone/protein lysine acetyltransferases
    • CrossRef PubMed
    • Berndsen, C.E. and Denu, J.M. (2008) Catalysis and substrate selection by histone/protein lysine acetyltransferases. Curr. Opin. Struct. Biol. 18, 682-689 CrossRef PubMed
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 682-689
    • Berndsen, C.E.1    Denu, J.M.2


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