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Volumn 109, Issue 22, 2012, Pages

Allosteric pathways in imidazole glycerol phosphate synthase

Author keywords

Generalized correlation analysis; Glutamine hydrolysis; Network theory; Protein networks

Indexed keywords

BACTERIAL ENZYME; ENZYME; GLUTAMINASE; HERBICIDE; HETERODIMER; HISTIDINE; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 84861889672     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1120536109     Document Type: Article
Times cited : (187)

References (30)
  • 1
    • 0035151834 scopus 로고    scopus 로고
    • Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase
    • DOI 10.1128/JB.182.3.989-996.2001
    • Klem TJ, Chen Y, Davisson VJ (2001) Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase. J Bacteriol 183:989-996. (Pubitemid 32095309)
    • (2001) Journal of Bacteriology , vol.183 , Issue.3 , pp. 989-996
    • Klem, T.J.1    Chen, Y.2    Davisson, V.J.3
  • 2
    • 0034793603 scopus 로고    scopus 로고
    • 8 barrel joins two active sites
    • DOI 10.1016/S0969-2126(01)00661-X, PII S096921260100661X
    • Chaudhuri BN, et al. (2001) Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)(8) barrel joins two active sites. Structure 9:987-997. (Pubitemid 32972164)
    • (2001) Structure , vol.9 , Issue.10 , pp. 987-997
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Chittur, S.V.4    Davisson, V.J.5    Smith, J.L.6
  • 3
    • 0038325358 scopus 로고    scopus 로고
    • Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: Open-closed conformational change and ammonia tunneling
    • Omi R, et al. (2002) Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunneling. J Biochem 132:759-765. (Pubitemid 35408499)
    • (2002) Journal of Biochemistry , vol.132 , Issue.5 , pp. 759-765
    • Omi, R.1    Mizuguchi, H.2    Goto, M.3    Miyahara, I.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7
  • 4
    • 0027254139 scopus 로고
    • Imidazole glycerol phosphate synthase: The glutamine amidotransferase in histidine biosynthesis
    • DOI 10.1021/bi00070a029
    • Klem TJ, Davisson VJ (1993) Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Biochemistry 32:5177-5186. (Pubitemid 23162087)
    • (1993) Biochemistry , vol.32 , Issue.19 , pp. 5177-5186
    • Klem, T.J.1    Davisson, V.J.2
  • 5
  • 6
    • 58049177333 scopus 로고    scopus 로고
    • Induction of protective immunity against Burkholderia pseudomallei using attenuated mutants with defects in the intracellular life cycle
    • Breitbach K, Kohler J, Steinmetz I (2008) Induction of protective immunity against Burkholderia pseudomallei using attenuated mutants with defects in the intracellular life cycle. Trans R Soc Trop Med Hyg 102:S89-S94.
    • (2008) Trans R Soc Trop Med Hyg , vol.102
    • Breitbach, K.1    Kohler, J.2    Steinmetz, I.3
  • 7
    • 33750580687 scopus 로고    scopus 로고
    • Genes involved in intrinsic antibiotic resistance of Acinetobacter baylyi
    • DOI 10.1128/AAC.00579-06
    • Gomez MJ, Neyfakh AA (2006) Genes involved in intrinsic antibiotic resistance of Acinetobacter baylyi. Antimicrob Agents Chemother 50:3562-3567. (Pubitemid 44684866)
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , Issue.11 , pp. 3562-3567
    • Gomez, M.J.1    Neyfakh, A.A.2
  • 8
    • 0037938734 scopus 로고    scopus 로고
    • Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase
    • DOI 10.1021/bi034314l
    • Myers RS, Jensen JR, Deras IL, Smith JL, Davisson VJ (2003) Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase. Biochemistry 42:7013-7022. (Pubitemid 36706484)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7013-7022
    • Myers, R.S.1    Jensen, J.R.2    Deras, I.L.3    Smith, J.L.4    Davisson, V.J.5
  • 11
    • 0038614879 scopus 로고    scopus 로고
    • Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: Crystal structures of a ternary complex and the free enzyme
    • DOI 10.1021/bi034320h
    • Chaudhuri BN, Lange SC, Myers RS, Davisson VJ, Smith JL (2003) Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerol-phosphate synthase: crystal structures of a ternary complex and the free enzyme. Biochemistry 42:7003-7012. (Pubitemid 36706483)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7003-7012
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Davisson, V.J.4    Smith, J.L.5
  • 12
    • 33847609615 scopus 로고    scopus 로고
    • A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase
    • DOI 10.1021/bi061708e
    • Amaro RE, Sethi A, Myers RS, Davisson VJ, Luthey-Schulten ZA (2007) A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase. Biochemistry 46:2156-2173. (Pubitemid 46355325)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2156-2173
    • Amaro, R.E.1    Sethi, A.2    Myers, R.S.3    Davisson, V.J.4    Luthey-Schulten, Z.A.5
  • 13
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE (1948) A mathematical theory of communication. AT&T Tech J 27:623-656.
    • (1948) AT&T Tech J , vol.27 , pp. 623-656
    • Shannon, C.E.1
  • 14
    • 78649766072 scopus 로고    scopus 로고
    • Nanometer propagation of millisecond motions in V-type allostery
    • Lipchock JM, Loria JP (2010) Nanometer propagation of millisecond motions in V-type allostery. Structure 18:1596-1607.
    • (2010) Structure , vol.18 , pp. 1596-1607
    • Lipchock, J.M.1    Loria, J.P.2
  • 15
    • 23244441019 scopus 로고    scopus 로고
    • Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase
    • DOI 10.1021/bi050706b
    • Myers RS, Amaro RE, Luthey-Schulten ZA, Davisson VJ (2005) Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry 44:11974-11985. (Pubitemid 41285695)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 11974-11985
    • Myers, R.S.1    Amaro, R.E.2    Luthey-Schulten, Z.A.3    Davisson, V.J.4
  • 16
    • 23244440559 scopus 로고    scopus 로고
    • Structural elements in IGP synthase exclude water to optimize ammonia transfer
    • DOI 10.1529/biophysj.104.058651
    • Amaro RE, Myers RS, Davisson VJ, Luthey-Schulten ZA (2005) Structural elements in IGP synthase exclude water to optimize ammonia transfer. Biophys J 89:475-487. (Pubitemid 41098302)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 475-487
    • Amaro, R.E.1    Myers, R.S.2    Davisson, V.J.3    Luthey-Schulten, Z.A.4
  • 17
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • DOI 10.1038/nsb0196-74
    • Tesmer JG, Klem TJ, Deras ML, Davisson VJ, Smith JL (1996) The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat Struct Biol 3:74-86. (Pubitemid 26023914)
    • (1996) Nature Structural Biology , vol.3 , Issue.1 , pp. 74-86
    • Tesmer, J.J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 18
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 angstrom from substrate to product
    • DOI 10.1021/bi970503q
    • Thoden JB, Holden HM, Wesenberg G, Raushel FM, Rayment I (1997) Structure of carbamoyl phosphate synthetase: a journey of 96 angstrom from substrate to product. Biochemistry 36:6305-6316. (Pubitemid 27231386)
    • (1997) Biochemistry , vol.36 , Issue.21 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 23
    • 0029092698 scopus 로고
    • Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular-dynamics simulations
    • Hunenberger PH, Mark AE, VangunsterenWF (1995) Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular-dynamics simulations. J Mol Biol 252:492-503.
    • (1995) J Mol Biol , vol.252 , pp. 492-503
    • Hunenberger, P.H.1    Mark, A.E.2    Vangunsteren, W.F.3
  • 24
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M (1991) Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 11:205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 26
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 27
    • 84945709831 scopus 로고
    • Algorithm-97-Shortest Path
    • Floyd RW (1962) Algorithm-97-Shortest Path. Commun Acm 5:345-345.
    • (1962) Commun Acm , vol.5 , pp. 345-345
    • Floyd, R.W.1
  • 29
    • 33745012299 scopus 로고    scopus 로고
    • Modularity and community structure in networks
    • Newman MEJ (2006) Modularity and community structure in networks. Proc Nat'l Acad Sci USA 103:8577-8582.
    • (2006) Proc Nat'l Acad Sci USA , vol.103 , pp. 8577-8582
    • Newman, M.E.J.1
  • 30
    • 0032898682 scopus 로고    scopus 로고
    • 2H-labeled proteins
    • DOI 10.1023/A:1008393201236
    • Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE (1999) A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated N-15-, C-13-, H-2-labeled proteins. J Biomol Nmr 13:369-374. (Pubitemid 29210329)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.4 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.