Structural highlights
Function
[SAMP1_HALVD] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation.
Publication Abstract from PubMed
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 beta-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.
Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.,Ye K, Liao S, Zhang W, Fan K, Zhang X, Zhang J, Xu C, Tu X Protein Sci. 2013 Sep;22(9):1174-82. doi: 10.1002/pro.2302. Epub 2013 Jul 22. PMID:23818097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2013 Sep;22(9):1174-82. doi: 10.1002/pro.2302. Epub 2013 Jul 22. PMID:23818097 doi:http://dx.doi.org/10.1002/pro.2302
