› 6vlj

Solution NMR

Solution NMR of Prochlorosin 2.8 produced by Prochlorococcus MIT 9313

Released:
DOI: 10.2210/pdb6vlj/pdb
PDB entry 6vlj coloured by chain, ensemble of 20 models, front view.
PDB entry 6vlj coloured by chain, ensemble of 20 models, side view.
PDB entry 6vlj coloured by chain, ensemble of 20 models, top view.
Source organism: Prochlorococcus marinus str. MIT 9313
Primary publication:
Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.
Bobeica SC, Zhu L, Acedo JZ, Tang W, van der Donk WA
Chem Sci 11 12854-12870 (2020)
PMID: 34094481

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nif11 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 19 amino acids
Theoretical weight: 2.06 KDa
Source organism: Prochlorococcus marinus str. MIT 9313
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7V447 (Residues: 65-83; Coverage: 23%)
Gene name: PMT_2122

Ligands and Environments

No bound ligands
1 modified residue:
Ligand DAL 2 x DAL

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 74%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.
Ongpipattanakul et al. (2022)
1 more

2 mentions without citation

Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.
Bobeica et al. (2020)
1 more