PDBsum entry 4xfv

Translation

PDB id: 4xfv

Contents

Protein chain

700 a.a.

Waters ×5

PDB id:

4xfv

Name:

Translation

Title:

Crystal structure of elp2

Structure:

Elongator complex protein 2. Chain: a. Synonym: gamma-toxin target 2, elp2. Engineered: yes

Source:

Saccharomyces cerevisiae s288c. Baker's yeast. Organism_taxid: 559292. Strain: s288c. Gene: elp2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.20Å R-factor: 0.199 R-free: 0.241

Authors:

Z.Lin,C.Dong,J.Long,Y.Shen

Key ref:

C.Dong et al. (2015). The Elp2 subunit is essential for elongator complex assembly and functional regulation. Structure, 23, 1078-1086. PubMed id: 25960406 DOI: 10.1016/j.str.2015.03.018

Date:

29-Dec-14 Release date: 20-May-15

Protein chain

P42935  (ELP2_YEAST) -  Elongator complex protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 788 a.a.

Struc: 700 a.a.

DOI no: 10.1016/j.str.2015.03.018

Structure 23:1078-1086 (2015)

PubMed id: 25960406

The Elp2 subunit is essential for elongator complex assembly and functional regulation.

C.Dong, Z.Lin, W.Diao, D.Li, X.Chu, Z.Wang, H.Zhou, Z.Xie, Y.Shen, J.Long.

ABSTRACT

Elongator is a highly conserved multiprotein complex composed of six subunits (Elp1-6). Elongator has been associated with various cellular activities and has attracted clinical attention because of its role in certain neurodegenerative diseases. Here, we present the crystal structure of the Elp2 subunit revealing two seven-bladed WD40 β propellers, and show by structure-guided mutational analyses that the WD40 fold integrity of Elp2 is necessary for its binding to Elp1 and Elp3 subunits in multiple species. The detailed biochemical experiments indicate that Elp2 binds microtubules through its conserved alkaline residues in vitro and in vivo. We find that both the mutually independent Elp2-mediated Elongator assembly and the cytoskeleton association are important for yeast viability. In addition, mutation of Elp2 greatly affects the histone H3 acetylation activity of Elongator in vivo. Our results indicate that Elp2 is a necessary component for functional Elongator and acts as a hub in the formation of various complexes.