2L83

A protein from Haloferax volcanii

Summary for 2L83

• Entry DOI: 10.2210/pdb2l83/pdb
• NMR Information: BMRB: 17391
• Descriptor: Small archaeal modifier protein 1 (1 entity in total)
• Functional Keywords: protein binding
• Biological source: Haloferax volcanii
• Total number of polymer chains: 1
• Total formula weight: 10014.93

Authors

Zhang, W.,Liao, S.,Fan, K.,Tu, X. (deposition date: 2011-01-03, release date: 2012-01-11, Last modification date: 2024-05-15)

Primary citation

Ye, K.,Liao, S.,Zhang, W.,Fan, K.,Zhang, X.,Zhang, J.,Xu, C.,Tu, X.
Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.
Protein Sci., 22:1174-1182, 2013

PubMed Abstract: Eukaryotic ubiquitin and ubiquitin-like systems play crucial roles in various cellular biological processes. In this work, we determined the solution structure of SAMP1 from Haloferax volcanii by NMR spectroscopy. Under low ionic conditions, SAMP1 presented two distinct conformations, one folded β-grasp and the other disordered. Interestingly, SAMP1 underwent a conformational conversion from disorder to order with ion concentration increasing, indicating that the ordered conformation is the functional form of SAMP1 under the physiological condition of H. volcanii. Furthermore, SAMP1 could interact with proteasome-activating nucleotidase B, supposing a potential role of SAMP1 in the protein degradation pathway mediated by proteasome.

PubMed: 23818097
DOI: 10.1002/pro.2302

Experimental method

SOLUTION NMR