메뉴 건너뛰기




Volumn 111, Issue 9, 2014, Pages 3389-3394

Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site

Author keywords

Membrane association; Proline catabolism; X ray crystallography

Indexed keywords

FLAVOPROTEIN; MEMBRANE PROTEIN; PROLINE; PROTEIN PUTA; QUERCETIN; QUINONE DERIVATIVE; UNCLASSIFIED DRUG; WATER;

EID: 84895795810     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1321621111     Document Type: Article
Times cited : (58)

References (31)
  • 2
    • 84859475161 scopus 로고    scopus 로고
    • Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolismto induce a transient ROS signal
    • Zarse K, et al. (2012) Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolismto induce a transient ROS signal. Cell Metab 15(4):451-465.
    • (2012) Cell Metab , vol.15 , Issue.4 , pp. 451-465
    • Zarse, K.1
  • 3
    • 84878604373 scopus 로고    scopus 로고
    • Reactive oxygen species homeostasis and virulence of the fungal pathogen Cryptococcus neoformans requires an intact proline catabolism pathway
    • Lee IR, et al. (2013) Reactive oxygen species homeostasis and virulence of the fungal pathogen Cryptococcus neoformans requires an intact proline catabolism pathway. Genetics 194(2):421-433.
    • (2013) Genetics , vol.194 , Issue.2 , pp. 421-433
    • Lee, I.R.1
  • 4
    • 46449111827 scopus 로고    scopus 로고
    • Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress
    • Krishnan N, Doster AR, Duhamel GE, Becker DF (2008) Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress. Infect Immun 76(7):3037-3044.
    • (2008) Infect Immun , vol.76 , Issue.7 , pp. 3037-3044
    • Krishnan, N.1    Doster, A.R.2    Duhamel, G.E.3    Becker, D.F.4
  • 5
    • 41149157883 scopus 로고    scopus 로고
    • Possible involvement of put A gene in Helicobacter pylori colonization in the stomach and motility
    • Nakajima K, et al. (2008) Possible involvement of put A gene in Helicobacter pylori colonization in the stomach and motility. Biomed Res 29(1):9-18.
    • (2008) Biomed Res , vol.29 , Issue.1 , pp. 9-18
    • Nakajima, K.1
  • 6
    • 84860314428 scopus 로고    scopus 로고
    • Unique structural features and sequence motifs of proline utilization A (PutA)
    • Singh RK, Tanner JJ (2012) Unique structural features and sequence motifs of proline utilization A (PutA). Front Biosci (Landmark Ed) 17:556-568.
    • (2012) Front Biosci (Landmark Ed) , vol.17 , pp. 556-568
    • Singh, R.K.1    Tanner, J.J.2
  • 7
    • 77649251784 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
    • Srivastava D, et al. (2010) Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum. Proc Natl Acad Sci USA 107(7): 2878-2883.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.7 , pp. 2878-2883
    • Srivastava, D.1
  • 8
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
    • Hura GL, et al. (2009) Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS). Nat Methods 6(8):606-612.
    • (2009) Nat Methods , vol.6 , Issue.8 , pp. 606-612
    • Hura, G.L.1
  • 9
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X, Holden HM, Raushel FM (2001) Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu Rev Biochem 70:149-180.
    • (2001) Annu Rev Biochem , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 10
    • 84864486886 scopus 로고    scopus 로고
    • MOLEonline 2. 0: Interactive web-based analysis of biomacromolecular channels
    • Berka K, et al. (2012) MOLEonline 2.0: Interactive web-based analysis of biomacromolecular channels. Nucleic Acids Res 40(Web Server issue):W222-W227.
    • (2012) Nucleic Acids Res , vol.40
    • Berka, K.1
  • 11
    • 84856946727 scopus 로고    scopus 로고
    • Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein
    • Moxley MA, Becker DF (2012) Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein. Biochemistry 51(1):511-520.
    • (2012) Biochemistry , vol.51 , Issue.1 , pp. 511-520
    • Moxley, M.A.1    Becker, D.F.2
  • 12
    • 84880625194 scopus 로고    scopus 로고
    • Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis
    • Serrano H, Blanchard JS (2013) Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis. Biochemistry 52(29):5009-5015.
    • (2013) Biochemistry , vol.52 , Issue.29 , pp. 5009-5015
    • Serrano, H.1    Blanchard, J.S.2
  • 13
    • 4744340116 scopus 로고    scopus 로고
    • Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
    • Zhang M, et al. (2004) Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Biochemistry 43(39):12539-12548.
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12539-12548
    • Zhang, M.1
  • 14
    • 84871285122 scopus 로고    scopus 로고
    • Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release
    • Luo M, Arentson BW, Srivastava D, Becker DF, Tanner JJ (2012) Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry 51(50):10099-10108.
    • (2012) Biochemistry , vol.51 , Issue.50 , pp. 10099-10108
    • Luo, M.1    Arentson, B.W.2    Srivastava, D.3    Becker, D.F.4    Tanner, J.J.5
  • 15
    • 33846185960 scopus 로고    scopus 로고
    • Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA-membrane binding
    • Zhang W, et al. (2007) Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA-membrane binding. Biochemistry 46(2):483-491.
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 483-491
    • Zhang, W.1
  • 16
    • 74949118627 scopus 로고    scopus 로고
    • The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction
    • Srivastava D, et al. (2010) The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. Biochemistry 49(3):560-569.
    • (2010) Biochemistry , vol.49 , Issue.3 , pp. 560-569
    • Srivastava, D.1
  • 17
    • 43949139276 scopus 로고    scopus 로고
    • Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine
    • White TA, Johnson WH, Jr., Whitman CP, Tanner JJ (2008) Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine. Biochemistry 47(20):5573-5580.
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5573-5580
    • White, T.A.1    Johnson Jr., W.H.2    Whitman, C.P.3    Tanner, J.J.4
  • 18
    • 59449094426 scopus 로고    scopus 로고
    • Polar lipid fatty acids, LPS-hydroxy fatty acids, and respiratory quinones of three Geobacter strains, and variation with electron acceptor
    • Hedrick DB, et al. (2009) Polar lipid fatty acids, LPS-hydroxy fatty acids, and respiratory quinones of three Geobacter strains, and variation with electron acceptor. J Ind Microbiol Biotechnol 36(2):205-209.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , Issue.2 , pp. 205-209
    • Hedrick, D.B.1
  • 19
    • 0037312937 scopus 로고    scopus 로고
    • Structureof the prolinedehydrogenase domain of the multifunctional PutA flavoprotein
    • LeeYH, Nadaraia S,GuD, Becker DF, Tanner JJ (2003) Structureof the prolinedehydrogenase domain of the multifunctional PutA flavoprotein. Nat Struct Biol 10(2):109-114.
    • (2003) Nat Struct Biol , vol.10 , Issue.2 , pp. 109-114
    • Lee, Y.H.1    Nadaraia, S.2    Gu, D.3    Becker, D.F.4    Tanner, J.J.5
  • 21
    • 36549013217 scopus 로고    scopus 로고
    • Conformational changes in ammoniachanneling glutamine amidotransferases
    • Mouilleron S, Golinelli-Pimpaneau B (2007) Conformational changes in ammoniachanneling glutamine amidotransferases. Curr Opin Struct Biol 17(6):653-664.
    • (2007) Curr Opin Struct Biol , vol.17 , Issue.6 , pp. 653-664
    • Mouilleron, S.1    Golinelli-Pimpaneau, B.2
  • 22
    • 84869083929 scopus 로고    scopus 로고
    • Structural insight into the type-II mitochondrial NADH dehydrogenases
    • Feng Y, et al. (2012) Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature 491(7424):478-482.
    • (2012) Nature , vol.491 , Issue.7424 , pp. 478-482
    • Feng, Y.1
  • 23
    • 84866533591 scopus 로고    scopus 로고
    • The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water-and lipid-soluble substrates
    • Iwata M, et al. (2012) The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water-and lipid-soluble substrates. Proc Natl Acad Sci USA 109(38):15247-15252.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.38 , pp. 15247-15252
    • Iwata, M.1
  • 24
    • 84861478324 scopus 로고    scopus 로고
    • Structure-activity characterization of sulfide:quinone oxidoreductase variants
    • Cherney MM, Zhang Y, James MN, Weiner JH (2012) Structure-activity characterization of sulfide:quinone oxidoreductase variants. J Struct Biol 178(3):319-328.
    • (2012) J Struct Biol , vol.178 , Issue.3 , pp. 319-328
    • Cherney, M.M.1    Zhang, Y.2    James, M.N.3    Weiner, J.H.4
  • 25
    • 0034724218 scopus 로고    scopus 로고
    • Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: Species comparison and structural changes with substrate binding and release
    • Faig M, et al. (2000) Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: Species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci USA 97(7):3177-3182.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3177-3182
    • Faig, M.1
  • 26
    • 0033520090 scopus 로고    scopus 로고
    • Crystal structure of human quinone reductase type 2, a metalloflavoprotein
    • Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM (1999) Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry 38(31):9881-9886.
    • (1999) Biochemistry , vol.38 , Issue.31 , pp. 9881-9886
    • Foster, C.E.1    Bianchet, M.A.2    Talalay, P.3    Zhao, Q.4    Amzel, L.M.5
  • 27
    • 81755173365 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism of the proline: Ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli
    • Moxley MA, Tanner JJ, Becker DF (2011) Steady-state kinetic mechanism of the proline: ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch Biochem Biophys 516(2):113-120.
    • (2011) Arch Biochem Biophys , vol.516 , Issue.2 , pp. 113-120
    • Moxley, M.A.1    Tanner, J.J.2    Becker, D.F.3
  • 28
    • 84859954420 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of the membraneembedded glycosyltransferase WaaA required for lipopolysaccharide synthesis
    • Schmidt H, et al. (2012) Structural and mechanistic analysis of the membraneembedded glycosyltransferase WaaA required for lipopolysaccharide synthesis. Proc Natl Acad Sci USA 109(16):6253-6258.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.16 , pp. 6253-6258
    • Schmidt, H.1
  • 29
    • 0034662927 scopus 로고    scopus 로고
    • The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme
    • Dym O, Pratt EA, Ho C, Eisenberg D (2000) The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc Natl Acad Sci USA 97(17):9413-9418.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.17 , pp. 9413-9418
    • Dym, O.1    Pratt, E.A.2    Ho, C.3    Eisenberg, D.4
  • 30
    • 67649872642 scopus 로고    scopus 로고
    • The structure of Aquifex aeolicus sulfide: Quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia M, Ermler U, Peng G, Michel H (2009) The structure of Aquifex aeolicus sulfide: quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106(24):9625-9630.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.24 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 31
    • 24944562717 scopus 로고    scopus 로고
    • Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy
    • Zhu W, Becker DF (2005) Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy. Biochemistry 44(37):12297-12306.
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12297-12306
    • Zhu, W.1    Becker, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.