› 7ry6

Solution NMR

Solution NMR structural bundle of the first cyclization domain from yersiniabactin synthetase (Cy1) impacted by dynamics

Released:
DOI: 10.2210/pdb7ry6/pdb
PDB entry 7ry6 coloured by chain, ensemble of 20 models, front view.
PDB entry 7ry6 coloured by chain, ensemble of 20 models, side view.
PDB entry 7ry6 coloured by chain, ensemble of 20 models, top view.
Source organism: Yersinia pestis
Primary publication:
Global protein dynamics as communication sensors in peptide synthetase domains.
Mishra SH, Kancherla AK, Marincin KA, Bouvignies G, Nerli S, Sgourakis N, Dowling DP, Frueh DP
Sci Adv 8 eabn6549 (2022)
PMID: 35857508

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104909 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Yersiniabactin biosynthetic protein Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 51.91 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2S9PH42 (Residues: 101-544; Coverage: 22%)
Gene names: YPO1911, irp2
Sequence domains: Condensation domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 52%
Refinement method: molecular dynamics
Expression system: Escherichia coli

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Citations

1 citations in other articles

High-resolution structures of a siderophore-producing cyclization domain from Yersinia pestis offer a refined proposal of substrate binding.
Gnann et al. (2022)

3 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
2 more