5M86

Crystal Structure of the Thermoplasma acidophilum Protein Ta1207

Summary for 5M86

• Entry DOI: 10.2210/pdb5m86/pdb
• Descriptor: Ta1207, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: pentamer, unknown function
• Biological source: Thermoplasma acidophilum DSM 1728
• Total number of polymer chains: 10
• Total formula weight: 395688.71

Authors

Pathare, G.R.,Nagy, I.,Bracher, A. (deposition date: 2016-10-28, release date: 2017-06-14, Last modification date: 2024-11-06)

Primary citation

Pathare, G.R.,Nagy, I.,Hubert, A.,Thomas, D.R.,Bracher, A.
Crystal structure of the Thermoplasma acidophilum protein Ta1207.
Acta Crystallogr F Struct Biol Commun, 73:328-335, 2017

PubMed 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 Å 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 α/β 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.

PubMed: 28580920
DOI: 10.1107/S2053230X17007087

Experimental method

X-RAY DIFFRACTION (2.4 Å)