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TitleBerberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity.
Journal, issue, pagesStructure, Vol. 32, Page 1429-, Year 2024
Publish dateMar 11, 2024 (structure data deposition date)
AuthorsBatool, Z. / Pavlova, J.A. / Paranjpe, M.N. / Tereshchenkov, A.G. / Lukianov, D.A. / Osterman, I.A. / Bogdanov, A.A. / Sumbatyan, N.V. / Polikanov, Y.S.
External linksStructure / PubMed:39019034
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-9b00:
Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with berberine analog of chloramphenicol CAM-BER, mRNA, deacylated A- and E-site tRNAphe, and deacylated P-site tRNAmet at 2.80A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

PDB-1aix:
HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL

ChemComp-ZN:
Unknown entry

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • thermus thermophilus hb8 (bacteria)
  • escherichia phage t4 (virus)
KeywordsRIBOSOME / Chloramphenicol; berberine; antibiotic; 70S ribosome; X-ray structure; translation inhibitor; binding affinity; peptidyl transferase center; nascent peptide exit tunnel

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