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Volumn 11, Issue 1, 2015, Pages 71-76

A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; NUCLEOPHILE; PHEGANOMYCIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; PEPTIDE;

EID: 84924925641     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1697     Document Type: Article
Times cited : (44)

References (46)
  • 1
    • 84884949156 scopus 로고    scopus 로고
    • A current perspective on daptomycin for the clinical microbiologist
    • Humphries, R.M., Pollett, S. & Sakoulas, G. A current perspective on daptomycin for the clinical microbiologist. Clin. Microbiol. Rev. 26, 759-780 (2013).
    • (2013) Clin. Microbiol. Rev , vol.26 , pp. 759-780
    • Humphries, R.M.1    Pollett, S.2    Sakoulas, G.3
  • 2
    • 84870918230 scopus 로고    scopus 로고
    • Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature
    • Arnison, P.G. et al. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature. Nat. Prod. Rep. 30, 108-160 (2013).
    • (2013) Nat. Prod. Rep , vol.30 , pp. 108-160
    • Arnison, P.G.1
  • 3
    • 68149132445 scopus 로고    scopus 로고
    • Structural insights into nonribosomal peptide enzymatic assembly lines
    • Koglin, A. & Walsh, C.T. Structural insights into nonribosomal peptide enzymatic assembly lines. Nat. Prod. Rep. 26, 987-1000 (2009).
    • (2009) Nat. Prod. Rep , vol.26 , pp. 987-1000
    • Koglin, A.1    Walsh, C.T.2
  • 4
    • 84863612987 scopus 로고    scopus 로고
    • Ribosome-independent biosynthesis of biologically active peptides: Application of synthetic biology to generate structural diversity
    • Giessen, T.W. & Marahiel, M.A. Ribosome-independent biosynthesis of biologically active peptides: application of synthetic biology to generate structural diversity. FEBS Lett. 586, 2065-2075 (2012).
    • (2012) FEBS Lett , vol.586 , pp. 2065-2075
    • Giessen, T.W.1    Marahiel, M.A.2
  • 5
    • 84865335226 scopus 로고    scopus 로고
    • A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis
    • Maruyama, C. et al. A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis. Nat. Chem. Biol. 8, 791-797 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 791-797
    • Maruyama, C.1
  • 6
    • 34548688717 scopus 로고    scopus 로고
    • A new family of ATP-dependent oligomerization-macrocyclization biocatalysts
    • Kadi, N., Oves-Costales, D., Barona-Gomez, F. & Challis, G.L. A new family of ATP-dependent oligomerization-macrocyclization biocatalysts. Nat. Chem. Biol. 3, 652-656 (2007).
    • (2007) Nat. Chem. Biol , vol.3 , pp. 652-656
    • Kadi, N.1    Oves-Costales, D.2    Barona-Gomez, F.3    Challis, G.L.4
  • 7
    • 0023893794 scopus 로고
    • Mode of action of deoxypheganomycin D on Mycobacterium smegmatis ATCC 607
    • Suzukake-Tsuchiya, K., Hori, M., Shimada, N. & Hamada, M. Mode of action of deoxypheganomycin D on Mycobacterium smegmatis ATCC 607. J. Antibiot. (Tokyo) 41, 675-683 (1988).
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 675-683
    • Suzukake-Tsuchiya, K.1    Hori, M.2    Shimada, N.3    Hamada, M.4
  • 8
    • 84868118472 scopus 로고    scopus 로고
    • Identification and characterisation of the gene cluster for the anti-MRSA antibiotic bottromycin: Expanding the biosynthetic diversity of ribosomal peptides
    • Crone, W.J.K., Leeper, F.J. & Truman, A.W. Identification and characterisation of the gene cluster for the anti-MRSA antibiotic bottromycin: expanding the biosynthetic diversity of ribosomal peptides. Chemical Science 3, 3516-3521 (2012).
    • (2012) Chemical Science , vol.3 , pp. 3516-3521
    • Crone, W.J.K.1    Leeper, F.J.2    Truman, A.W.3
  • 9
    • 84868104639 scopus 로고    scopus 로고
    • Synthetic biotechnology to study and engineer ribosomal bottromycin biosynthesis
    • Huo, L., Rachid, S., Stadler, M., Wenzel, S.C. & Muller, R. Synthetic biotechnology to study and engineer ribosomal bottromycin biosynthesis. Chem. Biol. 19, 1278-1287 (2012).
    • (2012) Chem. Biol , vol.19 , pp. 1278-1287
    • Huo, L.1    Rachid, S.2    Stadler, M.3    Wenzel, S.C.4    Muller, R.5
  • 11
    • 43749113148 scopus 로고    scopus 로고
    • A global assembly line for cyanobactins
    • Donia, M.S., Ravel, J. & Schmidt, E.W. A global assembly line for cyanobactins. Nat. Chem. Biol. 4, 341-343 (2008).
    • (2008) Nat. Chem. Biol , vol.4 , pp. 341-343
    • Donia, M.S.1    Ravel, J.2    Schmidt, E.W.3
  • 12
    • 0035910072 scopus 로고    scopus 로고
    • Glycopeptide antibiotic biosynthesis: Enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine
    • Chen, H., Tseng, C.C., Hubbard, B.K. & Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98, 14901-14906 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14901-14906
    • Chen, H.1    Tseng, C.C.2    Hubbard, B.K.3    Walsh, C.T.4
  • 13
    • 0023849634 scopus 로고
    • Replacement of Streptomyces hygroscopicus genomic segments with in vitro altered DNA sequences
    • Anzai, H. et al. Replacement of Streptomyces hygroscopicus genomic segments with in vitro altered DNA sequences. J. Antibiot. (Tokyo) 41, 226-233 (1988).
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 226-233
    • Anzai, H.1
  • 15
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi, H. et al. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution. J. Mol. Biol. 229, 1083-1100 (1993).
    • (1993) J. Mol. Biol , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1
  • 16
    • 0028860295 scopus 로고
    • A common fold for peptide synthetases cleaving ATP to ADP: Glutathione synthetase and D-alanine:D-alanine ligase of Escherichia coli
    • Fan, C., Moews, P.C., Shi, Y., Walsh, C.T. & Knox, J.R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:D-alanine ligase of Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 1172-1176 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1172-1176
    • Fan, C.1    Moews, P.C.2    Shi, Y.3    Walsh, C.T.4    Knox, J.R.5
  • 17
    • 22544447354 scopus 로고    scopus 로고
    • YwfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase
    • Tabata, K., Ikeda, H. & Hashimoto, S. ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase. J. Bacteriol. 187, 5195-5202 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 5195-5202
    • Tabata, K.1    Ikeda, H.2    Hashimoto, S.3
  • 18
    • 75649144445 scopus 로고    scopus 로고
    • A novel L-amino acid ligase from Bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis
    • Kino, K., Arai, T. & Tateiwa, D. A novel L-amino acid ligase from Bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis. Biosci. Biotechnol. Biochem. 74, 129-134 (2010).
    • (2010) Biosci. Biotechnol. Biochem , vol.74 , pp. 129-134
    • Kino, K.1    Arai, T.2    Tateiwa, D.3
  • 19
    • 61649088165 scopus 로고    scopus 로고
    • Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system
    • Taguchi, S., Mita, K., Ichinohe, K. & Hashimoto, S. Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system. Appl. Environ. Microbiol. 75, 1460-1464 (2009).
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 1460-1464
    • Taguchi, S.1    Mita, K.2    Ichinohe, K.3    Hashimoto, S.4
  • 20
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm, L. & Sander, C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20, 478-480 (1995).
    • (1995) Trends Biochem. Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 21
    • 77958037340 scopus 로고    scopus 로고
    • Crystal structure of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria
    • Sampei, G. et al. Crystal structure of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria. J. Biochem. 148, 429-438 (2010).
    • (2010) J. Biochem , vol.148 , pp. 429-438
    • Sampei, G.1
  • 22
    • 75149192731 scopus 로고    scopus 로고
    • Structural and functional studies of Aspergillus clavatus N5-carboxyaminoimidazole ribonucleotide synthetase
    • Thoden, J.B., Holden, H.M., Paritala, H. & Firestine, S.M. Structural and functional studies of Aspergillus clavatus N5-carboxyaminoimidazole ribonucleotide synthetase. Biochemistry 49, 752-760 (2010).
    • (2010) Biochemistry , vol.49 , pp. 752-760
    • Thoden, J.B.1    Holden, H.M.2    Paritala, H.3    Firestine, S.M.4
  • 24
    • 84867835695 scopus 로고    scopus 로고
    • The structure of L-amino-acid ligase from Bacillus licheniformis
    • Suzuki, M. et al. The structure of L-amino-acid ligase from Bacillus licheniformis. Acta Crystallogr. D Biol. Crystallogr. 68, 1535-1540 (2012).
    • (2012) Acta Crystallogr. D Biol. Crystallogr , vol.68 , pp. 1535-1540
    • Suzuki, M.1
  • 25
    • 0032506054 scopus 로고    scopus 로고
    • X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli
    • Wang, W., Kappock, T.J., Stubbe, J. & Ealick, S.E. X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Biochemistry 37, 15647-15662 (1998).
    • (1998) Biochemistry , vol.37 , pp. 15647-15662
    • Wang, W.1    Kappock, T.J.2    Stubbe, J.3    Ealick, S.E.4
  • 26
    • 0033976458 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman, A. et al. The Pfam protein families database. Nucleic Acids Res. 28, 263-266 (2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 263-266
    • Bateman, A.1
  • 27
    • 84878934964 scopus 로고    scopus 로고
    • Ubiquitin ligases and cell cycle control
    • Teixeira, L.K. & Reed, S.I. Ubiquitin ligases and cell cycle control. Annu. Rev. Biochem. 82, 387-414 (2013).
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 387-414
    • Teixeira, L.K.1    Reed, S.I.2
  • 28
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S.K., Liu, G., Ton-That, H. & Schneewind, O. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285, 760-763 (1999).
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 29
    • 0025226104 scopus 로고
    • Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase
    • Kane, P.M. et al. Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase. Science 250, 651-657 (1990).
    • (1990) Science , vol.250 , pp. 651-657
    • Kane, P.M.1
  • 30
    • 84863012427 scopus 로고    scopus 로고
    • Modification of N-terminal α-amino groups of peptides and proteins using ketenes
    • Chan, A.O. et al. Modification of N-terminal α-amino groups of peptides and proteins using ketenes. J. Am. Chem. Soc. 134, 2589-2598 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 2589-2598
    • Chan, A.O.1
  • 31
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S.E. & Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 32
    • 80053069963 scopus 로고    scopus 로고
    • N-terminal protein modification using simple aminoacyl transferase substrates
    • Wagner, A.M. et al. N-terminal protein modification using simple aminoacyl transferase substrates. J. Am. Chem. Soc. 133, 15139-15147 (2011).
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 15139-15147
    • Wagner, A.M.1
  • 33
    • 84883019327 scopus 로고    scopus 로고
    • N-terminal labeling of peptides by trypsin-catalyzed ligation for quantitative proteomics
    • Pan, Y. et al. N-terminal labeling of peptides by trypsin-catalyzed ligation for quantitative proteomics. Angew. Chem. Int. Edn Engl. 52, 9205-9209 (2013).
    • (2013) Angew. Chem. Int. Edn Engl , vol.52 , pp. 9205-9209
    • Pan, Y.1
  • 34
    • 0033736728 scopus 로고    scopus 로고
    • Preparation of N-formamidinylamino acids from amino and formamidinesulfinic acids
    • Jursic, B.S., Neumann, D. & McPherson, A. Preparation of N-formamidinylamino acids from amino and formamidinesulfinic acids. Synthesis 32, 1656-1658 (2000).
    • (2000) Synthesis , vol.32 , pp. 1656-1658
    • Jursic, B.S.1    Neumann, D.2    McPherson, A.3
  • 35
    • 43149115851 scopus 로고    scopus 로고
    • Velvet: Algorithms for de novo short read assembly using de Bruijn graphs
    • Zerbino, D.R. & Birney, E. Velvet: algorithms for de novo short read assembly using de Bruijn graphs. Genome Res. 18, 821-829 (2000).
    • (2000) Genome Res , vol.18 , pp. 821-829
    • Zerbino, D.R.1    Birney, E.2
  • 36
    • 59149090570 scopus 로고    scopus 로고
    • MetaGeneAnnotator: Detecting species-specific patterns of ribosomal binding site for precise gene prediction in anonymous prokaryotic and phage genomes
    • Noguchi, H., Taniguchi, T. & Itoh, T. MetaGeneAnnotator: detecting species-specific patterns of ribosomal binding site for precise gene prediction in anonymous prokaryotic and phage genomes. DNA Res. 15, 387-396 (2008).
    • (2008) DNA Res , vol.15 , pp. 387-396
    • Noguchi, H.1    Taniguchi, T.2    Itoh, T.3
  • 37
    • 0024419124 scopus 로고
    • Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus)
    • Vara, J., Lewandowska-Skarbek, M., Wang, Y.G., Donadio, S. & Hutchinson, C.R. Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus). J. Bacteriol. 171, 5872-5881 (1989).
    • (1989) J. Bacteriol , vol.171 , pp. 5872-5881
    • Vara, J.1    Lewandowska-Skarbek, M.2    Wang, Y.G.3    Donadio, S.4    Hutchinson, C.R.5
  • 41
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 42
    • 84860273177 scopus 로고    scopus 로고
    • Towars automated crystallographic structure refinement with phenix. Refine
    • Afonine, P.V. et al. Towars automated crystallographic structure refinement with phenix. refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352-367 (2012).
    • (2012) Acta Crystallogr. D Biol. Crystallogr , vol.68 , pp. 352-367
    • Afonine, P.V.1
  • 44
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V.B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 45
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. Version 1.2 of the crystallography and NMR system. Nat. Protoc. 2, 2728-2733 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 46
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • Trott, O. & Olson, A.J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J. Comput. Chem. 31, 455-461 (2010).
    • (2010) J. Comput. Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2


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