› 1dcj

Solution NMR

SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION

Released:
DOI: 10.2210/pdb1dcj/pdb
PDB entry 1dcj coloured by chain, ensemble of 20 models, front view.
PDB entry 1dcj coloured by chain, ensemble of 20 models, side view.
PDB entry 1dcj coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.
Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T
J Mol Biol 304 219-29 (2000)
PMID: 11080457

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfur carrier protein TusA Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A890 (Residues: 1-81; Coverage: 100%)
Gene names: JW3435, b3470, sirA, tusA, yhhP
Sequence domains: Sulfurtransferase TusA
Structure domains: TusA-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: HYBRID DISTANCE GEOMETRY-SIMULATED ANNEALING
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Initiation of protein synthesis in bacteria.
Laursen et al. (2005)
1 more

12 mentions without citation

Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions.
Shi et al. (2010)
11 more