› 5o96

X-ray diffraction
2.3Å resolution

Structure of the putative methyltransferase Lpg2936 from Legionella pneumophila in complex with the bound cofactor SAM

Released:
DOI: 10.2210/pdb5o96/pdb
PDB entry 5o96 coloured by chain, front view.
PDB entry 5o96 coloured by chain, side view.
PDB entry 5o96 coloured by chain, top view.
Source organism: Legionella pneumophila
Primary publication:
Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases.
Pinotsis N, Waksman G
OpenAccess logo Protein Sci 26 2381-2391 (2017)
PMID: 28940762

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + uracil(1498) in 16S rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178564 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal RNA small subunit methyltransferase E Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 245 amino acids
Theoretical weight: 27.34 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZRE6 (Residues: 2-244; Coverage: 100%)
Gene name: lpg2936
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAM 8 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Unit cell:
a: 104.482Å b: 98.74Å c: 225.783Å
α: 90° β: 91.76° γ: 90°
R-values:
R R work R free
0.185 0.182 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Interfering with Autophagy: The Opposing Strategies Deployed by Legionella pneumophila and Coxiella burnetii Effector Proteins.
Thomas et al. (2020)
3 other articles

2 mentions without citation

Restriction of S-adenosylmethionine conformational freedom by knotted protein binding sites.
Perlinska et al. (2020)
1 more