› 2k32

Solution NMR

Truncated AcrA from Campylobacter jejuni for glycosylation studies

Released:
DOI: 10.2210/pdb2k32/pdb
PDB entry 2k32 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k32 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k32 coloured by chain, ensemble of 20 models, top view.
Source organism: Campylobacter jejuni
Primary publication:
NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation.
Slynko V, Schubert M, Numao S, Kowarik M, Aebi M, Allain FH
J Am Chem Soc 131 1274-81 (2009)
PMID: 19154179

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186044 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RND efflux pump membrane fusion protein barrel-sandwich domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 12.75 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8RTE5 (Residues: 61-210; Coverage: 32%)
Gene names: E8P16_04140, E8P16_10560, GNO00_03940, QQI97_001038, cmeA
Sequence domains: Barrel-sandwich domain of CusB or HlyD membrane-fusion

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Protein glycosylation in bacteria: sweeter than ever.
Nothaft et al. (2010)
12 more

5 mentions without citation

Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.
Symmons et al. (2015)
4 more