@misc{zhouAtomicStructuresBacteriocin2024,
  title = {Atomic Structures of a Bacteriocin Targeting {{Gram-positive}} Bacteria},
  author = {Zhou, Z. Hong and Cai, Xiaoying and He, Yao and Yu, Iris and Imani, Anthony and Scholl, Dean and Miller, Jeff},
  year = {2024},
  month = mar,
  issn = {2693-5015},
  doi = {10.21203/rs.3.rs-4007122/v1},
  urldate = {2024-06-13},
  abstract = {Due to envelope differences between Gram-positive and Gram-negative bacteria1, engineering precision bactericidal contractile nanomachines2 requires atomic-level understanding of their structures; however, only those killing a Gram-negative bacterium are currently known3,4. Here, we report the atomic structures of an engineered diffocin, a contractile syringe-like molecular machine that kills the Gram-positive bacterium Clostridioides difficile. Captured in one pre-contraction and two post-contraction states, each structure fashions six proteins in the bacteria-targeting baseplate, two proteins in the energy-storing trunk, and a collar protein linking the sheath with the membrane-penetrating tube. Compared to contractile machines targeting Gram-negative bacteria, major differences reside in the baseplate and contraction magnitude, consistent with differences between their targeted envelopes. The multifunctional hub-hydrolase protein connects the tube and baseplate and is positioned to degrade peptidoglycan during penetration. The full-length tape measure protein forms a coiled-coil helix bundle homotrimer spanning the entire length of the diffocin. Our study offers mechanical insights and principles for designing potent protein-based precision antibiotics.},
  file = {C:\Users\shervinnia\Zotero\storage\J9GEUA2Z\Zhou et al. - 2024 - Atomic structures of a bacteriocin targeting Gram-.pdf}
}

{"_id":"pyBkPiQ6xZF6pZTeQ","bibbaseid":"zhou-cai-he-yu-imani-scholl-miller-atomicstructuresofabacteriocintargetinggrampositivebacteria-2024","author_short":["Zhou, Z. H.","Cai, X.","He, Y.","Yu, I.","Imani, A.","Scholl, D.","Miller, J."],"bibdata":{"bibtype":"misc","type":"misc","title":"Atomic Structures of a Bacteriocin Targeting Gram-positive Bacteria","author":[{"propositions":[],"lastnames":["Zhou"],"firstnames":["Z.","Hong"],"suffixes":[]},{"propositions":[],"lastnames":["Cai"],"firstnames":["Xiaoying"],"suffixes":[]},{"propositions":[],"lastnames":["He"],"firstnames":["Yao"],"suffixes":[]},{"propositions":[],"lastnames":["Yu"],"firstnames":["Iris"],"suffixes":[]},{"propositions":[],"lastnames":["Imani"],"firstnames":["Anthony"],"suffixes":[]},{"propositions":[],"lastnames":["Scholl"],"firstnames":["Dean"],"suffixes":[]},{"propositions":[],"lastnames":["Miller"],"firstnames":["Jeff"],"suffixes":[]}],"year":"2024","month":"March","issn":"2693-5015","doi":"10.21203/rs.3.rs-4007122/v1","urldate":"2024-06-13","abstract":"Due to envelope differences between Gram-positive and Gram-negative bacteria1, engineering precision bactericidal contractile nanomachines2 requires atomic-level understanding of their structures; however, only those killing a Gram-negative bacterium are currently known3,4. Here, we report the atomic structures of an engineered diffocin, a contractile syringe-like molecular machine that kills the Gram-positive bacterium Clostridioides difficile. Captured in one pre-contraction and two post-contraction states, each structure fashions six proteins in the bacteria-targeting baseplate, two proteins in the energy-storing trunk, and a collar protein linking the sheath with the membrane-penetrating tube. Compared to contractile machines targeting Gram-negative bacteria, major differences reside in the baseplate and contraction magnitude, consistent with differences between their targeted envelopes. The multifunctional hub-hydrolase protein connects the tube and baseplate and is positioned to degrade peptidoglycan during penetration. The full-length tape measure protein forms a coiled-coil helix bundle homotrimer spanning the entire length of the diffocin. Our study offers mechanical insights and principles for designing potent protein-based precision antibiotics.","file":"C:\\Users\\shervinnia\\Zotero\\storage\\J9GEUA2Z\\Zhou et al. - 2024 - Atomic structures of a bacteriocin targeting Gram-.pdf","bibtex":"@misc{zhouAtomicStructuresBacteriocin2024,\n title = {Atomic Structures of a Bacteriocin Targeting {{Gram-positive}} Bacteria},\n author = {Zhou, Z. Hong and Cai, Xiaoying and He, Yao and Yu, Iris and Imani, Anthony and Scholl, Dean and Miller, Jeff},\n year = {2024},\n month = mar,\n issn = {2693-5015},\n doi = {10.21203/rs.3.rs-4007122/v1},\n urldate = {2024-06-13},\n abstract = {Due to envelope differences between Gram-positive and Gram-negative bacteria1, engineering precision bactericidal contractile nanomachines2 requires atomic-level understanding of their structures; however, only those killing a Gram-negative bacterium are currently known3,4. Here, we report the atomic structures of an engineered diffocin, a contractile syringe-like molecular machine that kills the Gram-positive bacterium Clostridioides difficile. Captured in one pre-contraction and two post-contraction states, each structure fashions six proteins in the bacteria-targeting baseplate, two proteins in the energy-storing trunk, and a collar protein linking the sheath with the membrane-penetrating tube. Compared to contractile machines targeting Gram-negative bacteria, major differences reside in the baseplate and contraction magnitude, consistent with differences between their targeted envelopes. The multifunctional hub-hydrolase protein connects the tube and baseplate and is positioned to degrade peptidoglycan during penetration. The full-length tape measure protein forms a coiled-coil helix bundle homotrimer spanning the entire length of the diffocin. Our study offers mechanical insights and principles for designing potent protein-based precision antibiotics.},\n file = {C:\\Users\\shervinnia\\Zotero\\storage\\J9GEUA2Z\\Zhou et al. - 2024 - Atomic structures of a bacteriocin targeting Gram-.pdf}\n}\n\n","author_short":["Zhou, Z. H.","Cai, X.","He, Y.","Yu, I.","Imani, A.","Scholl, D.","Miller, J."],"key":"zhouAtomicStructuresBacteriocin2024","id":"zhouAtomicStructuresBacteriocin2024","bibbaseid":"zhou-cai-he-yu-imani-scholl-miller-atomicstructuresofabacteriocintargetinggrampositivebacteria-2024","role":"author","urls":{},"metadata":{"authorlinks":{}}},"bibtype":"misc","biburl":"https://bibbase.org/network/files/2MtabhipmJFGQ7n9n","dataSources":["mrv2RSxFMmgGBMu4y"],"keywords":[],"search_terms":["atomic","structures","bacteriocin","targeting","gram","positive","bacteria","zhou","cai","he","yu","imani","scholl","miller"],"title":"Atomic Structures of a Bacteriocin Targeting Gram-positive Bacteria","year":2024}