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8SVB

Antimicrobial lasso peptide achromonodin-1

Summary for 8SVB
Entry DOI10.2210/pdb8svb/pdb
NMR InformationBMRB: 31086
DescriptorAchromonodin-1 (1 entity in total)
Functional Keywordsantimicrobial, lasso peptide, antibiotic
Biological sourceAchromobacter xylosoxidans
Total number of polymer chains1
Total formula weight3220.59
Authors
Carson, D.V.,Cheung-Lee, W.L.,So, L.,Link, A.J. (deposition date: 2023-05-16, release date: 2023-10-11, Last modification date: 2024-10-30)
Primary citationCarson, D.V.,Zhang, Y.,So, L.,Cheung-Lee, W.L.,Cartagena, A.J.,Darst, S.A.,Link, A.J.
Discovery, Characterization, and Bioactivity of the Achromonodins: Lasso Peptides Encoded by Achromobacter .
J.Nat.Prod., 86:2448-2456, 2023
Cited by
PubMed Abstract: Through genome mining efforts, two lasso peptide biosynthetic gene clusters (BGCs) within two different species of , a genus that contains pathogenic organisms that can infect patients with cystic fibrosis, were discovered. Using gene-refactored BGCs in , these lasso peptides, which were named achromonodin-1 and achromonodin-2, were heterologously expressed. Achromonodin-1 is naturally encoded by certain isolates from the sputum of patients with cystic fibrosis. The NMR structure of achromonodin-1 was determined, demonstrating that it is a threaded lasso peptide with a large loop and short tail structure, reminiscent of previously characterized lasso peptides that inhibit RNA polymerase (RNAP). Achromonodin-1 inhibits RNAP and has potent, focused activity toward , another isolate from the sputum of a cystic fibrosis patient. These efforts expand the repertoire of antimicrobial lasso peptides and provide insights into how isolates from certain ecological niches interact with each other.
PubMed: 37870195
DOI: 10.1021/acs.jnatprod.3c00536
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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