메뉴 건너뛰기




Volumn 12, Issue 11, 2016, Pages 973-979

Structural basis for precursor protein-directed ribosomal peptide macrocyclization

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MDNB PROTEIN; MDNC PROTEIN; PROTEIN PRECURSOR; PROTEINASE; UNCLASSIFIED DRUG; RIBOSOME PROTEIN;

EID: 84988735283     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2200     Document Type: Article
Times cited : (49)

References (46)
  • 1
    • 84962367258 scopus 로고    scopus 로고
    • Natural products as sources of new drugs from 1981 to 2014
    • Newman, D.J. & Cragg, G.M. Natural products as sources of new drugs from 1981 to 2014. J. Nat. Prod. 79, 629-661 (2016).
    • (2016) J. Nat. Prod. , vol.79 , pp. 629-661
    • Newman, D.J.1    Cragg, G.M.2
  • 2
    • 84926205808 scopus 로고    scopus 로고
    • The re-emergence of natural products for drug discovery in the genomics era
    • Harvey, A.L., Edrada-Ebel, R. & Quinn, R.J. The re-emergence of natural products for drug discovery in the genomics era. Nat. Rev. Drug Discov. 14, 111-129 (2015).
    • (2015) Nat. Rev. Drug Discov. , vol.14 , pp. 111-129
    • Harvey, A.L.1    Edrada-Ebel, R.2    Quinn, R.J.3
  • 3
    • 67649604461 scopus 로고    scopus 로고
    • Ribosomal peptide natural products: Bridging the ribosomal and nonribosomal worlds
    • McIntosh, J.A., Donia, M.S. & Schmidt, E.W. Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Nat. Prod. Rep. 26, 537-559 (2009).
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 537-559
    • McIntosh, J.A.1    Donia, M.S.2    Schmidt, E.W.3
  • 4
    • 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
  • 5
    • 84965034936 scopus 로고    scopus 로고
    • New insights into the biosynthetic logic of ribosomally synthesized and post-translationally modified peptide natural products
    • Ortega, M.A. & van der Donk, W.A. New insights into the biosynthetic logic of ribosomally synthesized and post-translationally modified peptide natural products. Cell Chem. Biol. 23, 31-44 (2016).
    • (2016) Cell Chem. Biol. , vol.23 , pp. 31-44
    • Ortega, M.A.1    Van Der-Donk, W.A.2
  • 6
    • 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. Chem. Sci. (Camb.) 3, 3516 (2012).
    • (2012) Chem. Sci. (Camb.) , vol.3 , pp. 3516
    • Crone, W.J.K.1    Leeper, F.J.2    Truman, A.W.3
  • 7
    • 0942268866 scopus 로고    scopus 로고
    • Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
    • Xie, L. et al. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity. Science 303, 679-681 (2004).
    • (2004) Science , vol.303 , pp. 679-681
    • Xie, L.1
  • 8
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T.J. & van der Donk, W.A. Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat. Chem. Biol. 6, 9-18 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der-Donk, W.A.2
  • 9
    • 79953852240 scopus 로고    scopus 로고
    • Sequence diversity in the lasso peptide framework: Discovery of functional microcin J25 variants with multiple amino acid substitutions
    • Pan, S.J. & Link, A.J. Sequence diversity in the lasso peptide framework: discovery of functional microcin J25 variants with multiple amino acid substitutions. J. Am. Chem. Soc. 133, 5016-5023 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5016-5023
    • Pan, S.J.1    Link, A.J.2
  • 10
    • 84897436581 scopus 로고    scopus 로고
    • Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions
    • Weiz, A.R. et al. Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions. Angew. Chem. Int. Ed. Engl. 53, 3735-3738 (2014).
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 3735-3738
    • Weiz, A.R.1
  • 11
    • 84899485714 scopus 로고    scopus 로고
    • Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides
    • Mathavan, I. et al. Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides. Nat. Chem. Biol. 10, 340-342 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 340-342
    • Mathavan, I.1
  • 12
    • 84959018604 scopus 로고    scopus 로고
    • Metabolic model for diversity-generating biosynthesis
    • Tianero, M.D. et al. Metabolic model for diversity-generating biosynthesis. Proc. Natl. Acad. Sci. USA 113, 1772-1777 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 1772-1777
    • Tianero, M.D.1
  • 14
    • 82255186661 scopus 로고    scopus 로고
    • Leader peptide and a membrane protein scaffold guide the biosynthesis of the tricyclic peptide microviridin
    • Weiz, A.R. et al. Leader peptide and a membrane protein scaffold guide the biosynthesis of the tricyclic peptide microviridin. Chem. Biol. 18, 1413-1421 (2011).
    • (2011) Chem. Biol. , vol.18 , pp. 1413-1421
    • Weiz, A.R.1
  • 16
    • 84884205422 scopus 로고    scopus 로고
    • Structure and function of Escherichia coli RimK, an ATP-grasp fold, l-glutamyl ligase enzyme
    • Zhao, G. et al. Structure and function of Escherichia coli RimK, an ATP-grasp fold, l-glutamyl ligase enzyme. Proteins 81, 1847-1854 (2013).
    • (2013) Proteins , vol.81 , pp. 1847-1854
    • Zhao, G.1
  • 17
    • 72949106699 scopus 로고    scopus 로고
    • Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: Synthesis of novel metabolites and peptide modifications of proteins
    • Iyer, L.M., Abhiman, S., Maxwell Burroughs, A. & Aravind, L. Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: synthesis of novel metabolites and peptide modifications of proteins. Mol. Biosyst. 5, 1636-1660 (2009).
    • (2009) Mol. Biosyst. , vol.5 , pp. 1636-1660
    • Iyer, L.M.1    Abhiman, S.2    Maxwell Burroughs, A.3    Aravind, L.4
  • 19
    • 84875453542 scopus 로고    scopus 로고
    • Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus
    • Ouchi, T. et al. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9, 277-283 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 277-283
    • Ouchi, T.1
  • 20
    • 33750045457 scopus 로고    scopus 로고
    • Allosteric inhibition of Staphylococcus aureus d-alanine:d-alanine ligase revealed by crystallographic studies
    • Liu, S. et al. Allosteric inhibition of Staphylococcus aureus d-alanine:d-alanine ligase revealed by crystallographic studies. Proc. Natl. Acad. Sci. USA 103, 15178-15183 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15178-15183
    • Liu, S.1
  • 21
    • 83655198346 scopus 로고    scopus 로고
    • Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding
    • Wang, H., Falck, J.R., Hall, T.M.T. & Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8, 111-116 (2011).
    • (2011) Nat. Chem. Biol. , vol.8 , pp. 111-116
    • Wang, H.1    Falck, J.R.2    Hall, T.M.T.3    Shears, S.B.4
  • 22
    • 4143064981 scopus 로고    scopus 로고
    • Cyanobacterial protease inhibitor microviridin J causes a lethal molting disruption in Daphnia pulicaria
    • Rohrlack, T., Christoffersen, K., Kaebernick, M. & Neilan, B.A. Cyanobacterial protease inhibitor microviridin J causes a lethal molting disruption in Daphnia pulicaria. Appl. Environ. Microbiol. 70, 5047-5050 (2004).
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5047-5050
    • Rohrlack, T.1    Christoffersen, K.2    Kaebernick, M.3    Neilan, B.A.4
  • 23
    • 82255181183 scopus 로고    scopus 로고
    • Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases
    • Liu, Y., Zheng, T. & Bruner, S.D. Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases. Chem. Biol. 18, 1482-1488 (2011).
    • (2011) Chem. Biol. , vol.18 , pp. 1482-1488
    • Liu, Y.1    Zheng, T.2    Bruner, S.D.3
  • 24
    • 84864709843 scopus 로고    scopus 로고
    • The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain
    • Koehnke, J. et al. The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain. Nat. Struct. Mol. Biol. 19, 767-772 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 767-772
    • Koehnke, J.1
  • 25
    • 84940495619 scopus 로고    scopus 로고
    • Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence
    • Wang, B., Zhao, A., Novick, R.P. & Muir, T.W. Key driving forces in the biosynthesis of autoinducing peptides required for staphylococcal virulence. Proc. Natl. Acad. Sci. USA 112, 10679-10684 (2015).
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 10679-10684
    • Wang, B.1    Zhao, A.2    Novick, R.P.3    Muir, T.W.4
  • 26
    • 84856587556 scopus 로고    scopus 로고
    • Construction of a single polypeptide that matures and exports the lasso peptide microcin J25
    • Pan, S.J., Rajniak, J., Cheung, W.L. & Link, A.J. Construction of a single polypeptide that matures and exports the lasso peptide microcin J25. Chem Bio Chem 13, 367-370 (2012).
    • (2012) Chem Bio Chem , vol.13 , pp. 367-370
    • Pan, S.J.1    Rajniak, J.2    Cheung, W.L.3    Link, A.J.4
  • 27
    • 84860319350 scopus 로고    scopus 로고
    • An engineered lantibiotic synthetase that does not require a leader peptide on its substrate
    • Oman, T.J., Knerr, P.J., Bindman, N.A., Velásquez, J.E. & van der Donk, W.A. An engineered lantibiotic synthetase that does not require a leader peptide on its substrate. J. Am. Chem. Soc. 134, 6952-6955 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6952-6955
    • Oman, T.J.1    Knerr, P.J.2    Bindman, N.A.3    Velásquez, J.E.4    Van Der-Donk, W.A.5
  • 28
    • 84937395423 scopus 로고    scopus 로고
    • Structural analysis of leader peptide binding enables leader-free cyanobactin processing
    • Koehnke, J. et al. Structural analysis of leader peptide binding enables leader-free cyanobactin processing. Nat. Chem. Biol. 11, 558-563 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 558-563
    • Koehnke, J.1
  • 29
    • 84925460979 scopus 로고    scopus 로고
    • Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB
    • Ortega, M.A. et al. Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB. Nature 517, 509-512 (2015).
    • (2015) Nature , vol.517 , pp. 509-512
    • Ortega, M.A.1
  • 30
    • 84937438220 scopus 로고    scopus 로고
    • A prevalent peptide-binding domain guides ribosomal natural product biosynthesis
    • Burkhart, B.J., Hudson, G.A., Dunbar, K.L. & Mitchell, D.A. A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nat. Chem. Biol. 11, 564-570 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 564-570
    • Burkhart, B.J.1    Hudson, G.A.2    Dunbar, K.L.3    Mitchell, D.A.4
  • 31
    • 84940538541 scopus 로고    scopus 로고
    • The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold
    • Dong, S.-H. et al. The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold. eLife 4, e07607 (2015).
    • (2015) ELife , vol.4 , pp. e07607
    • Dong, S.-H.1
  • 32
    • 77950438898 scopus 로고    scopus 로고
    • Much of the microcin J25 leader peptide is dispensable
    • Cheung, W.L., Pan, S.J. & Link, A.J. Much of the microcin J25 leader peptide is dispensable. J. Am. Chem. Soc. 132, 2514-2515 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2514-2515
    • Cheung, W.L.1    Pan, S.J.2    Link, A.J.3
  • 33
    • 67649292568 scopus 로고    scopus 로고
    • Substrate specificity and scope of MvdD, a GRASP-like ligase from the microviridin biosynthetic gene cluster
    • Philmus, B., Guerrette, J.P. & Hemscheidt, T.K. Substrate specificity and scope of MvdD, a GRASP-like ligase from the microviridin biosynthetic gene cluster. ACS Chem. Biol. 4, 429-434 (2009).
    • (2009) ACS Chem. Biol. , vol.4 , pp. 429-434
    • Philmus, B.1    Guerrette, J.P.2    Hemscheidt, T.K.3
  • 34
    • 18844410256 scopus 로고    scopus 로고
    • Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella
    • Schmidt, E.W. et al. Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. Proc. Natl. Acad. Sci. USA 102, 7315-7320 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7315-7320
    • Schmidt, E.W.1
  • 35
    • 84861840835 scopus 로고    scopus 로고
    • High-precision isothermal titration calorimetry with automated peak-shape analysis
    • Keller, S. et al. High-precision isothermal titration calorimetry with automated peak-shape analysis. Anal. Chem. 84, 5066-5073 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 5066-5073
    • Keller, S.1
  • 37
    • 0242629052 scopus 로고    scopus 로고
    • Substructure search procedures for macromolecular structures
    • Adams, P.D. Substructure search procedures for macromolecular structures. Acta Crystallogr. Sect. D Biol. Crystallogr. 1966-1973 (2003).
    • (2003) Acta Crystallogr. Sect. D Biol. Crystallogr , pp. 1966-1973
    • Adams, P.D.1
  • 38
    • 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
  • 40
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 41
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G.N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 42
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers, F. et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1
  • 43
    • 57049150788 scopus 로고    scopus 로고
    • The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures
    • Goldenberg, O., Erez, E., Nimrod, G. & Ben-Tal, N. The ConSurf-DB: pre-calculated evolutionary conservation profiles of protein structures. Nucleic Acids Res. 37, D323-D327 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. D323-D327
    • Goldenberg, O.1    Erez, E.2    Nimrod, G.3    Ben-Tal, N.4
  • 45
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T.J. et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1
  • 46
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris, G.M. et al. AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J. Comput. Chem. 30, 2785-2791 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 2785-2791
    • Morris, G.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.