메뉴 건너뛰기




Volumn 7, Issue 2, 2012, Pages

Tetrahydrodipicolinate N-Succinyltransferase and dihydrodipicolinate synthase from Pseudomonas aeruginosa: Structure analysis and gene deletion

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIHYDRODIPICOLINATE SYNTHASE; RECOMBINANT PROTEIN; SUCCINYL COENZYME A; TETRAHYDRODIPICOLINATE N SUCCINYLTRANSFERASE; UNCLASSIFIED DRUG; ACYLTRANSFERASE; HYDROLYASE; SUCCINYL-COA-TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE;

EID: 84857130281     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0031133     Document Type: Article
Times cited : (20)

References (44)
  • 1
    • 77954469348 scopus 로고    scopus 로고
    • Multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii: resistance mechanisms and implications for therapy
    • Zavascki AP, Carvalhaes CG, Picão RC, Gales AC, (2010) Multidrug-resistant Pseudomonas aeruginosa and Acinetobacter baumannii: resistance mechanisms and implications for therapy. Expert Rev Anti Infect Ther 8: 71-93.
    • (2010) Expert Rev Anti Infect Ther , vol.8 , pp. 71-93
    • Zavascki, A.P.1    Carvalhaes, C.G.2    Picão, R.C.3    Gales, A.C.4
  • 2
    • 33644504829 scopus 로고    scopus 로고
    • An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants
    • Liberati NT, Urbach JM, Miyata S, Lee DG, Drenkard E, et al. (2006) An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants. Proc Natl Acad Sci U S A 103: 2833-2838.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2833-2838
    • Liberati, N.T.1    Urbach, J.M.2    Miyata, S.3    Lee, D.G.4    Drenkard, E.5
  • 3
    • 34250692637 scopus 로고    scopus 로고
    • Inhibition of lysine biosynthesis: an evolving antibiotic strategy
    • Hutton CA, Perugini MA, Gerrard JA, (2007) Inhibition of lysine biosynthesis: an evolving antibiotic strategy. Mol Biosyst 3: 458-465.
    • (2007) Mol Biosyst , vol.3 , pp. 458-465
    • Hutton, C.A.1    Perugini, M.A.2    Gerrard, J.A.3
  • 4
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti CM, Rubin EJ, (2003) Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci U S A 100: 12989-12994.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 5
    • 10344230938 scopus 로고    scopus 로고
    • Biosynthesis of diaminopimelate, the precursor of lysine and a component of peptidoglycan, is an essential function of Mycobacterium smegmatis
    • Pavelka MS Jr, Jacobs WR Jr, (1996) Biosynthesis of diaminopimelate, the precursor of lysine and a component of peptidoglycan, is an essential function of Mycobacterium smegmatis. J Bacteriol 178: 6496-6507.
    • (1996) J Bacteriol , vol.178 , pp. 6496-6507
    • Pavelka Jr., M.S.1    Jacobs Jr., W.R.2
  • 6
    • 33645030241 scopus 로고    scopus 로고
    • Robust Salmonella metabolism limits possibilities for new antimicrobials
    • Becker D, Selbach M, Rollenhagen C, Ballmaier M, Meyer TF, et al. (2006) Robust Salmonella metabolism limits possibilities for new antimicrobials. Nature 440: 303-307.
    • (2006) Nature , vol.440 , pp. 303-307
    • Becker, D.1    Selbach, M.2    Rollenhagen, C.3    Ballmaier, M.4    Meyer, T.F.5
  • 8
    • 0031012162 scopus 로고    scopus 로고
    • Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy
    • Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, et al. (1997) Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36: 24-33.
    • (1997) Biochemistry , vol.36 , pp. 24-33
    • Blickling, S.1    Renner, C.2    Laber, B.3    Pohlenz, H.D.4    Holak, T.A.5
  • 9
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 Å resolution
    • Mirwaldt C, Korndörfer I, Huber R, (1995) The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 Å resolution. J Mol Biol 246: 227-39.
    • (1995) J Mol Biol , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndörfer, I.2    Huber, R.3
  • 10
    • 30344464699 scopus 로고    scopus 로고
    • Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1.94 A resolution
    • Blagova E, Levdikov V, Milioti N, Fogg MJ, Kalliomaa AK, et al. (2006) Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1.94 A resolution. Proteins 62: 297-301.
    • (2006) Proteins , vol.62 , pp. 297-301
    • Blagova, E.1    Levdikov, V.2    Milioti, N.3    Fogg, M.J.4    Kalliomaa, A.K.5
  • 11
    • 67349221170 scopus 로고    scopus 로고
    • Cloning and characterization of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis
    • Devenish SR, Huisman FH, Parker EJ, Hadfield AT, Gerrard JA, (2009) Cloning and characterization of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis. Biochim Biophys Acta 1794: 1168-74.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1168-1174
    • Devenish, S.R.1    Huisman, F.H.2    Parker, E.J.3    Hadfield, A.T.4    Gerrard, J.A.5
  • 12
    • 25144446271 scopus 로고    scopus 로고
    • The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance
    • Dobson RC, Griffin MD, Jameson GB, Gerrard JA, (2005) The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crystallogr D61: 1116-24.
    • (2005) Acta Crystallogr , vol.D61 , pp. 1116-1124
    • Dobson, R.C.1    Griffin, M.D.2    Jameson, G.B.3    Gerrard, J.A.4
  • 13
    • 79960467869 scopus 로고    scopus 로고
    • A tetrameric structure is not essential for activity in dihydrodipicolinate synthase (DHDPS) from Mycobacterium tuberculosis
    • Evans G, Schuldt L, Griffin MD, Devenish SR, Grant Pearce F, et al. (2011) A tetrameric structure is not essential for activity in dihydrodipicolinate synthase (DHDPS) from Mycobacterium tuberculosis. Arch Biochem Biophys 512: 154-9.
    • (2011) Arch Biochem Biophys , vol.512 , pp. 154-159
    • Evans, G.1    Schuldt, L.2    Griffin, M.D.3    Devenish, S.R.4    Grant Pearce, F.5
  • 14
    • 42449110007 scopus 로고    scopus 로고
    • Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis
    • Kefala G, Evans GL, Griffin MD, Devenish SR, Pearce FG, et al. (2008) Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis. Biochem J 411: 351-60.
    • (2008) Biochem J , vol.411 , pp. 351-360
    • Kefala, G.1    Evans, G.L.2    Griffin, M.D.3    Devenish, S.R.4    Pearce, F.G.5
  • 16
    • 56349118584 scopus 로고    scopus 로고
    • Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein
    • Rice EA, Bannon GA, Glenn KC, Jeong SS, Sturman EJ, et al. (2008) Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein. Arch Biochem Biophys 480: 111-21.
    • (2008) Arch Biochem Biophys , vol.480 , pp. 111-121
    • Rice, E.A.1    Bannon, G.A.2    Glenn, K.C.3    Jeong, S.S.4    Sturman, E.J.5
  • 17
    • 77949314517 scopus 로고    scopus 로고
    • Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax
    • Voss JE, Scally SW, Taylor NL, Atkinson SC, Griffin MD, et al. (2010) Substrate-mediated stabilization of a tetrameric drug target reveals Achilles heel in anthrax. J Biol Chem 285: 5188-95.
    • (2010) J Biol Chem , vol.285 , pp. 5188-5195
    • Voss, J.E.1    Scally, S.W.2    Taylor, N.L.3    Atkinson, S.C.4    Griffin, M.D.5
  • 18
    • 55549137411 scopus 로고    scopus 로고
    • Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen
    • Burgess BR, Dobson RC, Bailey MF, Atkinson SC, Griffin MD, et al. (2008) Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen. J Biol Chem 283: 27598-603.
    • (2008) J Biol Chem , vol.283 , pp. 27598-27603
    • Burgess, B.R.1    Dobson, R.C.2    Bailey, M.F.3    Atkinson, S.C.4    Griffin, M.D.5
  • 19
    • 48749085398 scopus 로고    scopus 로고
    • Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
    • Girish TS, Sharma E, Gopal B, (2008) Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase. FEBS Lett 582: 2923-30.
    • (2008) FEBS Lett , vol.582 , pp. 2923-2930
    • Girish, T.S.1    Sharma, E.2    Gopal, B.3
  • 20
    • 79955835071 scopus 로고    scopus 로고
    • Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa
    • Kaur N, Gautam A, Kumar S, Singh A, Singh N, et al. (2011) Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa. Int J Biol Macromol 48: 779-787.
    • (2011) Int J Biol Macromol , vol.48 , pp. 779-787
    • Kaur, N.1    Gautam, A.2    Kumar, S.3    Singh, A.4    Singh, N.5
  • 21
    • 67649444194 scopus 로고    scopus 로고
    • Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis
    • Dobson RC, Perugini MA, Jameson GB, Gerrard JA, (2009) Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis. Biochimie 91: 1036-1044.
    • (2009) Biochimie , vol.91 , pp. 1036-1044
    • Dobson, R.C.1    Perugini, M.A.2    Jameson, G.B.3    Gerrard, J.A.4
  • 22
    • 25444488497 scopus 로고    scopus 로고
    • Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase
    • Dobson RC, Devenish SR, Turner LA, Clifford VR, Pearce FG, et al. (2005) Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase. Biochemistry 44: 13007-13013.
    • (2005) Biochemistry , vol.44 , pp. 13007-13013
    • Dobson, R.C.1    Devenish, S.R.2    Turner, L.A.3    Clifford, V.R.4    Pearce, F.G.5
  • 24
    • 0022993447 scopus 로고
    • Studies on the active site of succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Characterization using analogs of tetrahydrodipicolinate
    • Berges DA, DeWolf WE Jr, Dunn GL, Newman DJ, Schmidt SJ, et al. (1986) Studies on the active site of succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. Characterization using analogs of tetrahydrodipicolinate. J Biol Chem 261: 6160-6167.
    • (1986) J Biol Chem , vol.261 , pp. 6160-6167
    • Berges, D.A.1    DeWolf Jr., W.E.2    Dunn, G.L.3    Newman, D.J.4    Schmidt, S.J.5
  • 25
    • 39649099147 scopus 로고    scopus 로고
    • Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding
    • Nguyen L, Kozlov G, Gehring K, (2008) Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding. FEBS Lett 582: 623-626.
    • (2008) FEBS Lett , vol.582 , pp. 623-626
    • Nguyen, L.1    Kozlov, G.2    Gehring, K.3
  • 26
    • 67349208429 scopus 로고    scopus 로고
    • The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism
    • Schuldt L, Weyand S, Kefala G, Weiss MS, (2009) The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism. J Mol Biol 389: 863-879.
    • (2009) J Mol Biol , vol.389 , pp. 863-879
    • Schuldt, L.1    Weyand, S.2    Kefala, G.3    Weiss, M.S.4
  • 27
    • 0031026466 scopus 로고    scopus 로고
    • Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase
    • Beaman TW, Binder DA, Blanchard JS, Roderick SL, (1997) Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase. Biochemistry 36: 489-494.
    • (1997) Biochemistry , vol.36 , pp. 489-494
    • Beaman, T.W.1    Binder, D.A.2    Blanchard, J.S.3    Roderick, S.L.4
  • 28
    • 0032555280 scopus 로고    scopus 로고
    • The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase
    • Beaman TW, Blanchard JS, Roderick SL, (1998) The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase. Biochemistry 37: 10363-10369.
    • (1998) Biochemistry , vol.37 , pp. 10363-10369
    • Beaman, T.W.1    Blanchard, J.S.2    Roderick, S.L.3
  • 29
  • 30
    • 0029061955 scopus 로고
    • An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa
    • Schweizer HP, Hoang T, (1995) An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa. Gene 158: 15-22.
    • (1995) Gene , vol.158 , pp. 15-22
    • Schweizer, H.P.1    Hoang, T.2
  • 31
    • 64549143788 scopus 로고    scopus 로고
    • An improved Escherichia coli donor strain for diparental mating
    • Thoma S, Schobert M, (2009) An improved Escherichia coli donor strain for diparental mating. FEMS Microbiol Lett 294: 127-132.
    • (2009) FEMS Microbiol Lett , vol.294 , pp. 127-132
    • Thoma, S.1    Schobert, M.2
  • 32
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang TT, Karkhoff-Schweizer RR, Kutchma AJ, Schweizer HP, (1998) A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212: 77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 33
    • 0023607375 scopus 로고
    • A mouse model of chronic pulmonary infection with Pseudomonas aeruginosa and Pseudomonas cepacia
    • Starke JR, Edwards MS, Langston C, Baker CJ, (1987) A mouse model of chronic pulmonary infection with Pseudomonas aeruginosa and Pseudomonas cepacia. Pediatric Research 22: 698-702.
    • (1987) Pediatric Research , vol.22 , pp. 698-702
    • Starke, J.R.1    Edwards, M.S.2    Langston, C.3    Baker, C.J.4
  • 35
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP
    • Vagin A, Teplyakov A, (2010) Molecular replacement with MOLREP. Acta Crystallogr D66: 22-25.
    • (2010) Acta Crystallogr , vol.D66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ, (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D53: 240-255.
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 41
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J, (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16: 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 42
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 43
    • 0030444352 scopus 로고    scopus 로고
    • The diverse world of coenzyme A binding proteins
    • Engel C, Wierenga R, (1996) The diverse world of coenzyme A binding proteins. Curr Opin Struct Biol 6: 790-797.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 790-797
    • Engel, C.1    Wierenga, R.2
  • 44
    • 0000268861 scopus 로고
    • Calculation of an OMIT map
    • Bhat TN, (1988) Calculation of an OMIT map. J Appl Cryst 21: 279-281.
    • (1988) J Appl Cryst , vol.21 , pp. 279-281
    • Bhat, T.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.