› 6kwl

X-ray diffraction
1.8Å resolution

Crystal structure of pSLA-1*0401(R156A) complex with FMDV-derived epitope MTAHITVPY

Released:
DOI: 10.2210/pdb6kwl/pdb
PDB entry 6kwl coloured by chain, front view.
PDB entry 6kwl coloured by chain, side view.
PDB entry 6kwl coloured by chain, top view.
Source organisms:
Primary publication:
Peptidomes and Structures Illustrate Two Distinguishing Mechanisms of Alternating the Peptide Plasticity Caused by Swine MHC Class I Micropolymorphism.
Wei X, Wang S, Li Z, Li Z, Qu Z, Wang S, Zou B, Liang R, Xia C, Zhang N
Front Immunol 12 592447 (2021)
PMID: 33717070

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-101275 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.6 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0F6N4U7 (Residues: 22-296; Coverage: 81%)
Sequence domains:
Beta-2-microglobulin Chain: B
Molecule details ›
Chain: B
Length: 98 amino acids
Theoretical weight: 11.43 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07717 (Residues: 21-118; Coverage: 100%)
Gene name: B2M
Sequence domains: Immunoglobulin C1-set domain
Capsid protein VP2 Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 1.03 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Not provided
UniProt:
  • Canonical: P03311 (Residues: 440-448; Coverage: 0%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P21
Unit cell:
a: 49.039Å b: 66.201Å c: 57.032Å
α: 90° β: 107.91° γ: 90°
R-values:
R R work R free
0.196 0.193 0.247
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

New vistas unfold: Chicken MHC molecules reveal unexpected ways to present peptides to the immune system.
Halabi et al. (2022)
1 other article

1 mention without citation

Peptidomes and Structures Illustrate Two Distinguishing Mechanisms of Alternating the Peptide Plasticity Caused by Swine MHC Class I Micropolymorphism.
Wei et al. (2021)