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Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7.

Zahn M, Kieslich B, Berthold N, Knappe D, Hoffmann R, Strater N
Protein Pept Lett 21 407-12 (2014)
Related entries: 4jwc, 4jwd, 4jwi

Cited: 15 times
EuropePMC logo PMID: 24164259

Abstract

Bacterial resistance against common antibiotics is an increasing health problem. New pharmaceuticals for the treatment of infections caused by resistant pathogens are needed. Small proline-rich antimicrobial peptides (PrAMPs) from insects are known to bind intracellularly to the conventional substrate binding cleft of the E. coli Hsp70 chaperone DnaK. Furthermore, bactenecins from mammals, members of the cathelicidin family, also contain potential DnaK binding sites. Crystal structures of bovine and sheep Bac7 in complex with the DnaK substrate binding domain show that the peptides bind in the forward binding mode with a leucine positioned in the central hydrophobic pocket. In most structures, proline and arginine residues preceding leucine occupy the hydrophobic DnaK binding sites -1 and -2. Within bovine Bac7, four potential DnaK binding sites were identified.

Reviews citing this publication (6)

  1. Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria. Li W, Tailhades J, O'Brien-Simpson NM, Separovic F, Otvos L, Hossain MA, Wade JD. Amino Acids 46 2287-2294 (2014)
  2. Proline-rich antimicrobial peptides targeting protein synthesis. Graf M, Mardirossian M, Nguyen F, Seefeldt AC, Guichard G, Scocchi M, Innis CA, Wilson DN. Nat Prod Rep 34 702-711 (2017)
  3. Non-Lytic Antibacterial Peptides That Translocate Through Bacterial Membranes to Act on Intracellular Targets. Cardoso MH, Meneguetti BT, Costa BO, Buccini DF, Oshiro KGN, Preza SLE, Carvalho CME, Migliolo L, Franco OL. Int J Mol Sci 20 E4877 (2019)
  4. Emerging peptide antibiotics with therapeutic potential. Upert G, Luther A, Obrecht D, Ermert P. Med Drug Discov 9 100078 (2021)
  5. Snake Venom Cathelicidins as Natural Antimicrobial Peptides. de Barros E, Gonçalves RM, Cardoso MH, Santos NC, Franco OL, Cândido ES. Front Pharmacol 10 1415 (2019)
  6. Translocation of non-lytic antimicrobial peptides and bacteria penetrating peptides across the inner membrane of the bacterial envelope. Frimodt-Møller J, Campion C, Nielsen PE, Løbner-Olesen A. Curr Genet 68 83-90 (2022)

Articles citing this publication (9)

  1. The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Roy RN, Lomakin IB, Gagnon MG, Steitz TA. Nat Struct Mol Biol 22 466-469 (2015)
  2. The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex. Seefeldt AC, Nguyen F, Antunes S, Pérébaskine N, Graf M, Arenz S, Inampudi KK, Douat C, Guichard G, Wilson DN, Innis CA. Nat Struct Mol Biol 22 470-475 (2015)
  3. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Gagnon MG, Roy RN, Lomakin IB, Florin T, Mankin AS, Steitz TA. Nucleic Acids Res 44 2439-2450 (2016)
  4. Minibactenecins ChBac7.Nα and ChBac7. Nβ - Antimicrobial Peptides from Leukocytes of the Goat Capra hircus. Shamova OV, Orlov DS, Zharkova MS, Balandin SV, Yamschikova EV, Knappe D, Hoffmann R, Kokryakov VN, Ovchinnikova TV. Acta Naturae 8 136-146 (2016)
  5. Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity. Jeon D, Jeong MC, Jacob B, Bang JK, Kim EH, Cheong C, Jung ID, Park Y, Kim Y. Sci Rep 7 1455 (2017)
  6. Caprine Bactenecins as Promising Tools for Developing New Antimicrobial and Antitumor Drugs. Kopeikin PM, Zharkova MS, Kolobov AA, Smirnova MP, Sukhareva MS, Umnyakova ES, Kokryakov VN, Orlov DS, Milman BL, Balandin SV, Panteleev PV, Ovchinnikova TV, Komlev AS, Tossi A, Shamova OV. Front Cell Infect Microbiol 10 552905 (2020)
  7. Systematic Mutagenesis of Oncocin Reveals Enhanced Activity and Insights into the Mechanisms of Antimicrobial Activity. Lai PK, Geldart K, Ritter S, Kaznessis YN, Hackel BJ. Mol Syst Des Eng 3 930-941 (2018)
  8. Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones. Nordquist EB, English CA, Clerico EM, Sherman W, Gierasch LM, Chen J. PLoS Comput Biol 17 e1009567 (2021)
  9. Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future. Nordquist EB, Clerico EM, Chen J, Gierasch LM. J Phys Chem B 126 6780-6791 (2022)


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