› 3vlu

X-ray diffraction
1.55Å resolution

Crystal structure of Sphingomonas sp. A1 alginate-binding protein AlgQ1 in complex with saturated trimannuronate

Released:
DOI: 10.2210/pdb3vlu/pdb
PDB entry 3vlu coloured by chain, front view.
PDB entry 3vlu coloured by chain, side view.
PDB entry 3vlu coloured by chain, top view.
Source organism: Sphingomonas sp. A1
Primary publication:
Recognition of heteropolysaccharide alginate by periplasmic solute-binding proteins of a bacterial ABC transporter.
Nishitani Y, Maruyama Y, Itoh T, Mikami B, Hashimoto W, Murata K
Biochemistry 51 3622-33 (2012)
PMID: 22486720

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Extracellular solute-binding protein Chain: A
Molecule details ›
Chain: A
Length: 502 amino acids
Theoretical weight: 57.97 KDa
Source organism: Sphingomonas sp. A1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KWT6 (Residues: 25-526; Coverage: 99%)
Gene name: algQ1
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: BEM
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 58.472Å b: 67.52Å c: 61.663Å
α: 90° β: 94.58° γ: 90°
R-values:
R R work R free
0.192 0.191 0.213
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Conformational and dynamic plasticity in substrate-binding proteins underlies selective transport in ABC importers.
de Boer et al. (2019)
8 more

2 mentions without citation

Alginate-dependent gene expression mechanism in Sphingomonas sp. strain A1.
Hayashi et al. (2014)
1 more