› 6q50

X-ray diffraction
1.6Å resolution

Structure of MPT-4, a mannose phosphorylase from Leishmania mexicana, in complex with phosphate ion

Released:
DOI: 10.2210/pdb6q50/pdb
PDB entry 6q50 coloured by chain, front view.
PDB entry 6q50 coloured by chain, side view.
PDB entry 6q50 coloured by chain, top view.
Source organism: Leishmania mexicana MHOM/GT/2001/U1103
Primary publication:
A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites.
Sernee MF, Ralton JE, Nero TL, Sobala LF, Kloehn J, Vieira-Lara MA, Cobbold SA, Stanton L, Pires DEV, Hanssen E, Males A, Ward T, Bastidas LM, van der Peet PL, Parker MW, Ascher DB, Williams SJ, Davies GJ, McConville MJ
Cell Host Microbe 26 385-399.e9 (2019)
PMID: 31513773

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DUF1861 family protein Chain: A
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 37.6 KDa
Source organism: Leishmania mexicana MHOM/GT/2001/U1103
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9ANE0 (Residues: 1-315; Coverage: 100%)
Gene name: LMXM_10_1260
Sequence domains: Protein of unknown function (DUF1861)

Ligands and Environments

3 bound ligands:
Ligand PO4 1 x PO4
Ligand EDO 1 x EDO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Unit cell:
a: 53.366Å b: 67.194Å c: 96.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.2
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Paradigms of Protist/Bacteria Symbioses Affecting Human Health: Acanthamoeba species and Trichomonas vaginalis.
Henriquez et al. (2020)
3 more