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Volumn 51, Issue 21, 2012, Pages 4271-4279

Structural characterization of four prochlorosins: A novel class of lantipeptides produced by planktonic marine cyanobacteria

Author keywords

[No Author keywords available]

Indexed keywords

ASSIGNMENT OF; CYCLIC PEPTIDES; LANTHIONINES; LINEAR PEPTIDES; MARINE CYANOBACTERIA; NON-ENZYMATIC; NUCLEAR MAGNETIC RESONANCE STUDIES; POST-TRANSLATIONAL MODIFICATIONS; PROCHLOROCOCCUS; RING SIZES; RING TOPOLOGY; SECONDARY METABOLITES; STRUCTURAL CHARACTERIZATION; SYNTHETASES; THIOETHERS;

EID: 84861624891     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300255s     Document Type: Article
Times cited : (88)

References (48)
  • 1
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis, and engineering of lantipeptides
    • 101146/annurev-biochem-060110-113521
    • Knerr, P. J. and van der Donk, W. A. (2012) Discovery, biosynthesis, and engineering of lantipeptides Annu. Rev. Biochem. DOI: 10.1146/annurev-biochem- 060110-113521
    • (2012) Annu. Rev. Biochem.
    • Knerr, P.J.1    Van Der Donk, W.A.2
  • 2
    • 77950563372 scopus 로고    scopus 로고
    • Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights
    • Goto, Y., Li, B., Claesen, J., Shi, Y., Bibb, M. J., and van der Donk, W. A. (2010) Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights PLoS Biol. 8, e1000339
    • (2010) PLoS Biol. , vol.8 , pp. 1000339
    • Goto, Y.1    Li, B.2    Claesen, J.3    Shi, Y.4    Bibb, M.J.5    Van Der Donk, W.A.6
  • 3
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
    • Schnell, N., Entian, K.-D., Schneider, U., Götz, F., Zahner, H., Kellner, R., and Jung, G. (1988) Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings Nature 333, 276-278
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.-D.2    Schneider, U.3    Götz, F.4    Zahner, H.5    Kellner, R.6    Jung, G.7
  • 5
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J. and van der Donk, W. A. (2010) Follow the leader: The use of leader peptides to guide natural product biosynthesis Nat. Chem. Biol. 6, 9-18
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 7
    • 33645216333 scopus 로고    scopus 로고
    • Niche partitioning among Prochlorococcus ecotypes along ocean-scale environmental gradients
    • Johnson, Z. I., Zinser, E. R., Coe, A., McNulty, N. P., Woodward, E. M. S., and Chisholm, S. W. (2006) Niche partitioning among Prochlorococcus ecotypes along ocean-scale environmental gradients Science 311, 1737-1740
    • (2006) Science , vol.311 , pp. 1737-1740
    • Johnson, Z.I.1    Zinser, E.R.2    Coe, A.3    McNulty, N.P.4    Woodward, E.M.S.5    Chisholm, S.W.6
  • 8
    • 35848941716 scopus 로고    scopus 로고
    • Lantibiotics: Peptides of diverse structure and function
    • Willey, J. M. and van der Donk, W. A. (2007) Lantibiotics: Peptides of diverse structure and function Annu. Rev. Microbiol. 61, 477-501
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 477-501
    • Willey, J.M.1    Van Der Donk, W.A.2
  • 9
    • 77952511174 scopus 로고    scopus 로고
    • Expansion of ribosomally produced natural products: A nitrile hydratase- and Nif11-related precursor family
    • Haft, D. H., Basu, M. K., and Mitchell, D. A. (2010) Expansion of ribosomally produced natural products: A nitrile hydratase- and Nif11-related precursor family BMC Biol. 8, 70
    • (2010) BMC Biol. , vol.8 , pp. 70
    • Haft, D.H.1    Basu, M.K.2    Mitchell, D.A.3
  • 10
  • 11
    • 25744441978 scopus 로고
    • Resolution of sulfur-containing amino-acids by chiral phase gas-chromatography
    • Küsters, E., Allgaier, H., Jung, G., and Bayer, E. (1984) Resolution of sulfur-containing amino-acids by chiral phase gas-chromatography Chromatographia 18, 287-293
    • (1984) Chromatographia , vol.18 , pp. 287-293
    • Küsters, E.1    Allgaier, H.2    Jung, G.3    Bayer, E.4
  • 12
    • 80052580657 scopus 로고    scopus 로고
    • Solid supported chemical syntheses of both components of the lantibiotic lacticin 3147
    • Liu, W., Chan, A. S. H., Liu, H. Q., Cochrane, S. A., and Vederas, J. C. (2011) Solid supported chemical syntheses of both components of the lantibiotic lacticin 3147 J. Am. Chem. Soc. 133, 14216-14219
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14216-14219
    • Liu, W.1    Chan, A.S.H.2    Liu, H.Q.3    Cochrane, S.A.4    Vederas, J.C.5
  • 13
  • 15
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy J. Magn. Reson. 53, 521-528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 16
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sørensen, O. W., and Ernst, R. R. (1982) Multiple quantum filters for elucidating NMR coupling networks J. Am. Chem. Soc. 104, 6800-6801
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 17
    • 0343359244 scopus 로고
    • Investigation of exchange processes by 2-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by 2-dimensional NMR spectroscopy J. Chem. Phys. 71, 4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 19
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco.
    • Goddard, T. D. and Kneller, D. G. (2005) Sparky, University of California, San Francisco.
    • (2005) Sparky
    • Goddard, T.D.1    Kneller, D.G.2
  • 20
    • 80052092565 scopus 로고    scopus 로고
    • Nine post-translational modifications during the biosynthesis of cinnamycin
    • Ökesli, A., Cooper, L. E., Fogle, E. J., and van der Donk, W. A. (2011) Nine post-translational modifications during the biosynthesis of cinnamycin J. Am. Chem. Soc. 133, 13753-13760
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13753-13760
    • Ökesli, A.1    Cooper, L.E.2    Fogle, E.J.3    Van Der Donk, W.A.4
  • 21
    • 79960963680 scopus 로고    scopus 로고
    • Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate
    • Velásquez, J. E., Zhang, X. G., and van der Donk, W. A. (2011) Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate Chem. Biol. 18, 857-867
    • (2011) Chem. Biol. , vol.18 , pp. 857-867
    • Velásquez, J.E.1    Zhang, X.G.2    Van Der Donk, W.A.3
  • 23
    • 34548512831 scopus 로고    scopus 로고
    • Lantibiotic engineering: Molecular characterization and exploitation of lantibiotic-synthesizing enzymes for peptide engineering
    • Nagao, J., Aso, Y., Shioya, K., Nakayama, J., and Sonomoto, K. (2007) Lantibiotic engineering: Molecular characterization and exploitation of lantibiotic-synthesizing enzymes for peptide engineering J. Mol. Microbiol. Biotechnol. 13, 235-242
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 235-242
    • Nagao, J.1    Aso, Y.2    Shioya, K.3    Nakayama, J.4    Sonomoto, K.5
  • 24
    • 0010409139 scopus 로고
    • NMR and circular dichroism studies on Pep5
    • In (Jung, G. and Sahl, H. G. Eds.) pp, ESCOM, Leiden, The Netherlands.
    • Freund, S., Jung, G., Gibbons, W. A., and Sahl, H. G. (1991) NMR and circular dichroism studies on Pep5. In Nisin and Novel Lantibiotics (Jung, G. and Sahl, H. G., Eds.) pp 103-112, ESCOM, Leiden, The Netherlands.
    • (1991) Nisin and Novel Lantibiotics , pp. 103-112
    • Freund, S.1    Jung, G.2    Gibbons, W.A.3    Sahl, H.G.4
  • 26
    • 1542743956 scopus 로고    scopus 로고
    • Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity
    • Martin, N. I., Sprules, T., Carpenter, M. R., Cotter, P. D., Hill, C., Ross, R. P., and Vederas, J. C. (2004) Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity Biochemistry 43, 3049-3056
    • (2004) Biochemistry , vol.43 , pp. 3049-3056
    • Martin, N.I.1    Sprules, T.2    Carpenter, M.R.3    Cotter, P.D.4    Hill, C.5    Ross, R.P.6    Vederas, J.C.7
  • 28
    • 0033711399 scopus 로고    scopus 로고
    • Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics
    • Smith, L., Novak, J., Rocca, J., McClung, S., Hillman, J. D., and Edison, A. S. (2000) Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics Eur. J. Biochem. 267, 6810-6816
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6810-6816
    • Smith, L.1    Novak, J.2    Rocca, J.3    McClung, S.4    Hillman, J.D.5    Edison, A.S.6
  • 29
    • 50949105606 scopus 로고    scopus 로고
    • N-terminal acetylation in paenibacillin, a novel lantibiotic
    • He, Z., Yuan, C., Zhang, L., and Yousef, A. E. (2008) N-terminal acetylation in paenibacillin, a novel lantibiotic FEBS Lett. 582, 2787-2792
    • (2008) FEBS Lett. , vol.582 , pp. 2787-2792
    • He, Z.1    Yuan, C.2    Zhang, L.3    Yousef, A.E.4
  • 30
    • 0021028219 scopus 로고
    • Isolation and characterization of ancovenin, a new inhibitor of angiotensin i converting enzyme, produced by actinomycetes
    • Kido, Y., Hamakado, T., Yoshida, T., Anno, M., Motoki, Y., Wakamiya, T., and Shiba, T. (1983) Isolation and characterization of ancovenin, a new inhibitor of angiotensin I converting enzyme, produced by actinomycetes J. Antibiot. 36, 1295-1299
    • (1983) J. Antibiot. , vol.36 , pp. 1295-1299
    • Kido, Y.1    Hamakado, T.2    Yoshida, T.3    Anno, M.4    Motoki, Y.5    Wakamiya, T.6    Shiba, T.7
  • 32
    • 0027385948 scopus 로고
    • Model Studies of Lantibiotic Biogenesis
    • Toogood, P. L. (1993) Model Studies of Lantibiotic Biogenesis Tetrahedron Lett. 34, 7833-7836
    • (1993) Tetrahedron Lett. , vol.34 , pp. 7833-7836
    • Toogood, P.L.1
  • 34
    • 0034676587 scopus 로고    scopus 로고
    • Facile chemoselective synthesis of dehydroalanine-containing peptides
    • Okeley, N. M., Zhu, Y., and van der Donk, W. A. (2000) Facile chemoselective synthesis of dehydroalanine-containing peptides Org. Lett. 2, 3603-3606
    • (2000) Org. Lett. , vol.2 , pp. 3603-3606
    • Okeley, N.M.1    Zhu, Y.2    Van Der Donk, W.A.3
  • 35
    • 0037129424 scopus 로고    scopus 로고
    • Biomimetic stereoselective formation of methyllanthionine
    • Zhou, H. and van der Donk, W. A. (2002) Biomimetic stereoselective formation of methyllanthionine Org. Lett. 4, 1335-1338
    • (2002) Org. Lett. , vol.4 , pp. 1335-1338
    • Zhou, H.1    Van Der Donk, W.A.2
  • 36
    • 0142094530 scopus 로고    scopus 로고
    • Biomimetic studies on the mechanism of stereoselective lanthionine formation
    • Zhu, Y., Gieselman, M., Zhou, H., Averin, O., and van der Donk, W. A. (2003) Biomimetic studies on the mechanism of stereoselective lanthionine formation Org. Biomol. Chem. 1, 3304-3315
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3304-3315
    • Zhu, Y.1    Gieselman, M.2    Zhou, H.3    Averin, O.4    Van Der Donk, W.A.5
  • 37
    • 34548175995 scopus 로고    scopus 로고
    • On the regioselectivity of thioether formation by lacticin 481 synthetase
    • Zhang, X., Ni, W., and van der Donk, W. A. (2007) On the regioselectivity of thioether formation by lacticin 481 synthetase Org. Lett. 9, 3343-3346
    • (2007) Org. Lett. , vol.9 , pp. 3343-3346
    • Zhang, X.1    Ni, W.2    Van Der Donk, W.A.3
  • 38
    • 0142094530 scopus 로고    scopus 로고
    • Biomimetic studies on the mechanism of stereoselective lanthionine formation
    • Zhu, Y. T., Gieselman, M. D., Zhou, H., Averin, O., and van der Donk, W. A. (2003) Biomimetic studies on the mechanism of stereoselective lanthionine formation Org. Biomol. Chem. 1, 3304-3315
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3304-3315
    • Zhu, Y.T.1    Gieselman, M.D.2    Zhou, H.3    Averin, O.4    Van Der Donk, W.A.5
  • 39
    • 33847685140 scopus 로고    scopus 로고
    • On the substrate specificity of dehydration by lacticin 481 synthetase
    • Zhang, X. and van der Donk, W. A. (2007) On the substrate specificity of dehydration by lacticin 481 synthetase J. Am. Chem. Soc. 129, 2212-2213
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2212-2213
    • Zhang, X.1    Van Der Donk, W.A.2
  • 40
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins
    • Okeley, N. M., Paul, M., Stasser, J. P., Blackburn, N., and van der Donk, W. A. (2003) SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins Biochemistry 42, 13613-13624
    • (2003) Biochemistry , vol.42 , pp. 13613-13624
    • Okeley, N.M.1    Paul, M.2    Stasser, J.P.3    Blackburn, N.4    Van Der Donk, W.A.5
  • 41
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li, B., Yu, J. P., Brunzelle, J. S., Moll, G. N., van der Donk, W. A., and Nair, S. K. (2006) Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis Science 311, 1464-1467
    • (2006) Science , vol.311 , pp. 1464-1467
    • Li, B.1    Yu, J.P.2    Brunzelle, J.S.3    Moll, G.N.4    Van Der Donk, W.A.5    Nair, S.K.6
  • 42
    • 33947364360 scopus 로고    scopus 로고
    • Structure-function relationships of the lanthionine cyclase SpaC involved in biosynthesis of the Bacillus subtilis peptide antibiotic subtilin
    • Helfrich, M., Entian, K. D., and Stein, T. (2007) Structure-function relationships of the lanthionine cyclase SpaC involved in biosynthesis of the Bacillus subtilis peptide antibiotic subtilin Biochemistry 46, 3224-3233
    • (2007) Biochemistry , vol.46 , pp. 3224-3233
    • Helfrich, M.1    Entian, K.D.2    Stein, T.3
  • 43
    • 34547137156 scopus 로고    scopus 로고
    • Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin
    • Li, B. and van der Donk, W. A. (2007) Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin J. Biol. Chem. 282, 21169-21175
    • (2007) J. Biol. Chem. , vol.282 , pp. 21169-21175
    • Li, B.1    Van Der Donk, W.A.2
  • 44
    • 34249747857 scopus 로고    scopus 로고
    • Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity
    • Paul, M., Patton, G. C., and van der Donk, W. A. (2007) Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity Biochemistry 46, 6268-6276
    • (2007) Biochemistry , vol.46 , pp. 6268-6276
    • Paul, M.1    Patton, G.C.2    Van Der Donk, W.A.3
  • 45
    • 0000816291 scopus 로고    scopus 로고
    • Alkyl transfer to metal thiolates: Kinetics, active species identification, and relevance to the DNA methyl phosphotriester repair center of Escherichia coli Ada
    • Wilker, J. J. and Lippard, S. J. (1997) Alkyl transfer to metal thiolates: Kinetics, active species identification, and relevance to the DNA methyl phosphotriester repair center of Escherichia coli Ada Inorg. Chem. 36, 969-978
    • (1997) Inorg. Chem. , vol.36 , pp. 969-978
    • Wilker, J.J.1    Lippard, S.J.2
  • 46
    • 0034839228 scopus 로고    scopus 로고
    • Methylation of neutral pseudotetrahedral zinc thiolate complexes: Model reactions for alkyl group transfer to sulfur by zinc-containing enzymes
    • Warthen, C. R., Hammes, B. S., Carrano, C. J., and Crans, D. C. (2001) Methylation of neutral pseudotetrahedral zinc thiolate complexes: Model reactions for alkyl group transfer to sulfur by zinc-containing enzymes J. Biol. Inorg. Chem. 6, 82-90
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 82-90
    • Warthen, C.R.1    Hammes, B.S.2    Carrano, C.J.3    Crans, D.C.4
  • 47
    • 0035914908 scopus 로고    scopus 로고
    • Functional modeling of cobalamine-independent methionine synthase with pyrazolylborate-zinc-thiolate complexes
    • Brand, U., Rombach, M., Seebacher, J., and Vahrenkamp, H. (2001) Functional modeling of cobalamine-independent methionine synthase with pyrazolylborate-zinc-thiolate complexes Inorg. Chem. 40, 6151-6157
    • (2001) Inorg. Chem. , vol.40 , pp. 6151-6157
    • Brand, U.1    Rombach, M.2    Seebacher, J.3    Vahrenkamp, H.4
  • 48
    • 0037389593 scopus 로고    scopus 로고
    • Synthetic modeling of zinc thiolates: Quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates
    • Chiou, S. J., Riordan, C. G., and Rheingold, A. L. (2003) Synthetic modeling of zinc thiolates: Quantitative assessment of hydrogen bonding in modulating sulfur alkylation rates Proc. Natl. Acad. Sci. U.S.A. 100, 3695-3700
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3695-3700
    • Chiou, S.J.1    Riordan, C.G.2    Rheingold, A.L.3


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