PDBsum entry 5czy

Transferase

PDB id: 5czy

Contents

Protein chain

449 a.a.

Ligands

GOL ×3

SAM

Waters ×239

PDB id:

5czy

Name:

Transferase

Title:

Crystal structure of legas4

Structure:

Legionella effector legas4. Chain: a. Fragment: unp residues 63-545. Synonym: legas4, eukaryotic huntingtin interacting protein b. Engineered: yes

Source:

Legionella pneumophila subsp. Pneumophila str. Philadelphia 1. Organism_taxid: 272624. Strain: philadelphia 1. Gene: legas4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.205 R-free: 0.248

Authors:

J.Son,K.Y.Hwang,W.C.Lee

Key ref:

J.Son et al. (2015). Crystal structure of Legionella pneumophila type IV secretion system effector LegAS4. Biochem Biophys Res Commun, 465, 817-824. PubMed id: 26315269 DOI: 10.1016/j.bbrc.2015.08.094

Date:

01-Aug-15 Release date: 23-Sep-15

Protein chain

Q5ZUS4  (Q5ZUS4_LEGPH) -  Eukaryotic huntingtin interacting protein B from Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

Seq: 545 a.a.

Struc: 449 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.bbrc.2015.08.094

Biochem Biophys Res Commun 465:817-824 (2015)

PubMed id: 26315269

Crystal structure of Legionella pneumophila type IV secretion system effector LegAS4.

J.Son, C.H.Jo, R.N.Murugan, J.K.Bang, K.Y.Hwang, W.C.Lee.

ABSTRACT

The SET domain of LegAS4, a type IV secretion system effector of Legionella pneumophila, is a eukaryotic protein motif involved in histone methylation and epigenetic modulation. The SET domain of LegAS4 is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. Moreover, LegAS4 contains an ankyrin repeat domain of unknown function at its C-terminal region. Here, we report the crystal structure of LegAS4 in complex with S-adenosyl-l-methionine (SAM). Our data indicate that the ankyrin repeats interact extensively with the SET domain, especially with the SAM-binding amino acids, through conserved residues. Conserved surface analysis marks Glu159, Glu203, and Glu206 on the SET domain serve as candidate residues involved in interaction with the positively charged histone tail. Conserved surface residues on the ankyrin repeat domain surround a small pocket, which is suspected to serve as a binding site for an unknown ligand.