English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Crystal structure of the Thermoplasma acidophilum protein Ta1207

Pathare, G. R., Nagy, I., Hubert, A., Thomas, D. R., & Bracher, A. (2017). Crystal structure of the Thermoplasma acidophilum protein Ta1207. Acta Crystallographica Section F: Structural Biology Communications, 73, 328-335. doi:10.1107/S2053230X17007087.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E13A-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E13B-5
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Pathare, Ganesh Ramnath1, Author              
Nagy, Istvan1, Author              
Hubert, Agnes1, Author              
Thomas, Dennis R.1, Author              
Bracher, Andreas2, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

Content

show
hide
Free keywords: PROTEOMICS; REFINEMENT; SCATTERING; COMPLEXES; GENOMICS; SEQUENCEBiochemistry & Molecular Biology; Biophysics; Crystallography; pentamers; archaeon; thermostability; nanotechnology; Thermoplasma acidophilum; Ta1207;
 Abstract: The crystal structure of the Ta1207 protein from Thermoplasma acidophilum is reported. Ta1207 was identified in a screen for high-molecular-weight protein complexes in T. acidophilum. In solution, Ta1207 forms homopentamers of 188 kDa. The crystal structure of recombinant Ta1207 solved by Se-MAD at 2.4 angstrom resolution revealed a complex with fivefold symmetry. In the crystal lattice, calcium ions induce the formation of a nanocage from two pentamers. The Ta1207 protomers comprise two domains with the same novel alpha/beta topology. A deep pocket with a binding site for a negatively charged group suggests that Ta1207 functions as an intracellular receptor for an unknown ligand. Homologues of Ta1207 occur only in Thermoplasmatales and its function might be related to the extreme lifestyle of these archaea. The thermostable Ta1207 complex might provide a useful fivefold-symmetric scaffold for future nanotechnological applications.

Details

show
hide
Language(s): eng - English
 Dates: 2017-05-252017
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000402553700004
DOI: 10.1107/S2053230X17007087
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Acta Crystallographica Section F: Structural Biology Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 73 Sequence Number: - Start / End Page: 328 - 335 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1