› 6hyh

X-ray diffraction
2.5Å resolution

Crystal structure of MSMEG_1712 from Mycobacterium smegmatis in complex with Beta-D-Fucofuranose

Released:
DOI: 10.2210/pdb6hyh/pdb
PDB entry 6hyh coloured by chain, front view.
PDB entry 6hyh coloured by chain, side view.
PDB entry 6hyh coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Detection and Characterization of a Mycobacterial L-Arabinofuranose ABC Transporter Identified with a Rapid Lipoproteomics Protocol.
Li M, Müller C, Fröhlich K, Gorka O, Zhang L, Groß O, Schilling O, Einsle O, Jessen-Trefzer C
Cell Chem Biol 26 852-862.e6 (2019)
PMID: 31006617

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106310 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic binding protein domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 319 amino acids
Theoretical weight: 33.7 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0QT50 (Residues: 23-328; Coverage: 99%)
Gene name: MSMEG_1712
Sequence domains: Periplasmic binding protein domain

Ligands and Environments

2 bound ligands:
Ligand ZN 13 x ZN
Ligand GYE 2 x GYE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I4122
Unit cell:
a: 118.065Å b: 118.065Å c: 232.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.211 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope.
Jackson et al. (2021)
4 other articles

1 mention without citation

Characterization of the l-arabinofuranose-specific GafABCD ABC transporter essential for l-arabinose-dependent growth of the lignocellulose-degrading bacterium Shewanella sp. ANA-3.
Drousiotis et al. (2023)