› 5ioo

X-ray diffraction
2.52Å resolution

Accommodation of massive sequence variation in Nanoarchaeota by the C-type lectin fold

Released:
DOI: 10.2210/pdb5ioo/pdb
PDB 5ioo coloured by chain and viewed from the front.
PDB 5ioo coloured by chain and viewed from the side.
PDB 5ioo coloured by chain and viewed from the top.
Source organism: Nanoarchaeota archaeon JGI OTU-1
Primary publication:
Conservation of the C-type lectin fold for accommodating massive sequence variation in archaeal diversity-generating retroelements.
Handa S, Paul BG, Miller JF, Valentine DL, Ghosh P
BMC Struct. Biol. 16 13 (2016)
PMID: 27578274

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AvpA Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 28.7 KDa
Source organism: Nanoarchaeota archaeon JGI OTU-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1L1QK08 (Residues: 1-255; Coverage: 100%)

Ligands and Environments

1 bound ligand:
Ligand MG 4 x MG
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P61
Unit cell:
a: 143.998Å b: 143.998Å c: 59.261Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.202 0.25
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Prokaryotic reverse transcriptases: from retroelements to specialized defense systems.
González-Delgado et al. (2021)
1 more