› 4lnv

X-ray diffraction
3.7Å resolution

Crystal Structure of TEP1s

Released:
DOI: 10.2210/pdb4lnv/pdb
PDB entry 4lnv coloured by chain, front view.
PDB entry 4lnv coloured by chain, side view.
PDB entry 4lnv coloured by chain, top view.
Source organism: Anopheles gambiae
Primary publication:
Molecular basis for genetic resistance of Anopheles gambiae to Plasmodium: structural analysis of TEP1 susceptible and resistant alleles.
Le BV, Williams M, Logarajah S, Baxter RH
PLoS Pathog 8 e1002958 (2012)
PMID: 23055931

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Thioester-containing protein 1 allele S1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 1323 amino acids
Theoretical weight: 150.69 KDa
Source organism: Anopheles gambiae
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9GYW4 (Residues: 22-1338; Coverage: 100%)
Gene names: TEP-I, TEP1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 15 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43
Unit cell:
a: 196.472Å b: 196.472Å c: 225.267Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.237 0.276
Expression system: Trichoplusia ni

Quick links

Citations

4 review citations

Arthropod Innate Immune Systems and Vector-Borne Diseases.
Baxter et al. (2017)
3 more

1 mention without citation

The structure and function of thioester-containing proteins in arthropods.
Williams et al. (2014)