PDBsum entry 5oap

Transcription

PDB id: 5oap

Contents

Protein chain

18 a.a.

PDB id:

5oap

Name:

Transcription

Title:

Solution nmr structure of dreb2a(255-272) bound to rcd1-rst

Structure:

Dreb2a. Chain: a. Engineered: yes. Other_details: residues 255-272

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: axx17_at5g04900. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

K.Bugge,L.Staby,K.Skriver,B.B.Kragelund

Key ref:

K.Bugge et al. (2018). Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common αα-Scaffold for Disorder in Transcriptional Networks. Structure, 26, 734. PubMed id: 29657132 DOI: 10.1016/j.str.2018.03.013

Date:

23-Jun-17 Release date: 18-Apr-18

Protein chain

O82132  (DRE2A_ARATH) -  Dehydration-responsive element-binding protein 2A from Arabidopsis thaliana

Seq: 335 a.a.

Struc: 18 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2018.03.013

Structure 26:734 (2018)

PubMed id: 29657132

Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common αα-Scaffold for Disorder in Transcriptional Networks.

K.Bugge, L.Staby, K.R.Kemplen, C.O'Shea, S.K.Bendsen, M.K.Jensen, J.G.Olsen, K.Skriver, B.B.Kragelund.

ABSTRACT

Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the αα hubs, as they share an αα-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity.