› 7veq

X-ray diffraction
1.7Å resolution

Crystal structure of bacterial chemotaxis-dependent pectin-binding protein SPH1118 in an open conformation

Released:
DOI: 10.2210/pdb7veq/pdb
PDB entry 7veq coloured by chain, front view.
PDB entry 7veq coloured by chain, side view.
PDB entry 7veq coloured by chain, top view.
Source organism: Sphingomonas sp. A1
Primary publication:
Substrate size-dependent conformational changes of bacterial pectin-binding protein crucial for chemotaxis and assimilation.
Anamizu K, Takase R, Hio M, Watanabe D, Mikami B, Hashimoto W
OpenAccess logo Sci Rep 12 12653 (2022)
PMID: 35879323

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-168988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SPH1118 Chain: A
Molecule details ›
Chain: A
Length: 609 amino acids
Theoretical weight: 68.78 KDa
Source organism: Sphingomonas sp. A1
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2221
Unit cell:
a: 50.855Å b: 151.663Å c: 179.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.195
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation.
Ohnuma et al. (2023)

1 mention without citation

Substrate size-dependent conformational changes of bacterial pectin-binding protein crucial for chemotaxis and assimilation.
Anamizu et al. (2022)