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TitlePeptide Recognition and Mechanism of the Radical S -Adenosyl-l-methionine Multiple Cyclophane Synthase ChlB.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 147, Page 16850-16863, Year 2025
Publish dateAug 28, 2024 (structure data deposition date)
AuthorsRuel, J. / Nguyen, T.Q.N. / Morishita, Y. / Usclat, A. / Martin, L. / Amara, P. / Kieffer-Jaquinod, S. / Stefanoiu, M.C. / de la Mora, E. / Morinaka, B.I. / Nicolet, Y.
External linksJ. Am. Chem. Soc. / PubMed:40354606
MethodsX-ray diffraction
Resolution1.653 - 1.77 Å
Structure data

PDB-9gm3:
Crystal structure of the complex formed between the radical SAM protein ChlB and the leader region of its precursor substrate ChlA
Method: X-RAY DIFFRACTION / Resolution: 1.653 Å

PDB-9gmc:
Crystal structure of the complex formed between the radical SAM protein ChlB and the R3A mutant of ChlA
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FMT:
FORMIC ACID

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

Source
  • fischerella (bacteria)
KeywordsOXIDOREDUCTASE / Radical SAM protein Ribosomal synthesized and post-translationally modified peptides Iron sulfur clusters Peptide binding protein / Radical SAM protein Ribosomally synthesised and post-translationally modified peptides Iron sulfur clusters Peptide binding protein

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