EMD-4095

Single-particle
22.7 Å
EMD-4095 Deposition: 08/08/2016
Map released: 17/08/2016
Last modified: 02/08/2017
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-4095

Negative stain EM-structure of Checkpoint point kinase Tel1

EMD-4095

Single-particle
22.7 Å
EMD-4095 Deposition: 08/08/2016
Map released: 17/08/2016
Last modified: 02/08/2017
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae S288c
Sample: Tel1 protein

Deposition Authors: Darbari VC, Sawicka M, Wanrooij PH, Hailemariam S, Zhang X, Burgers PM
The Dimeric Architecture of Checkpoint Kinases Mec1ATR and Tel1ATM Reveal a Common Structural Organization.
Sawicka M , Wanrooij PH , Darbari VC , Tannous E , Hailemariam S, Bose D , Makarova AV, Burgers PM, Zhang X
(2016) J. Biol. Chem. , 291 , 13436 - 13447
PUBMED: 27129217
DOI: doi:10.1074/jbc.M115.708263
ISSN: 1083-351X
ASTM: JBCHA3
Abstract:
The phosphatidylinositol 3-kinase-related protein kinases are key regulators controlling a wide range of cellular events. The yeast Tel1 and Mec1·Ddc2 complex (ATM and ATR-ATRIP in humans) play pivotal roles in DNA replication, DNA damage signaling, and repair. Here, we present the first structural insight for dimers of Mec1·Ddc2 and Tel1 using single-particle electron microscopy. Both kinases reveal a head to head dimer with one major dimeric interface through the N-terminal HEAT (named after Huntingtin, elongation factor 3, protein phosphatase 2A, and yeast kinase TOR1) repeat. Their dimeric interface is significantly distinct from the interface of mTOR complex 1 dimer, which oligomerizes through two spatially separate interfaces. We also observe different structural organizations of kinase domains of Mec1 and Tel1. The kinase domains in the Mec1·Ddc2 dimer are located in close proximity to each other. However, in the Tel1 dimer they are fully separated, providing potential access of substrates to this kinase, even in its dimeric form.