4WWM

X-ray crystal structure of Sulfolobus solfataricus Urm1

Summary for 4WWM

• Entry DOI: 10.2210/pdb4wwm/pdb
• Descriptor: Uncharacterized protein, SULFATE ION (3 entities in total)
• Functional Keywords: ubiquitin-like, modifier, archaea, signaling protein
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 2
• Total formula weight: 21617.13

Authors

Bray, S.M.,Anjum, S.R.,Blackwood, J.K.,Kilkenny, M.L.,Coelho, M.A.,Foster, B.M.,Pellegrini, L.,Robinson, N.P. (deposition date: 2014-11-11, release date: 2015-09-23, Last modification date: 2024-05-08)

Primary citation

Anjum, R.S.,Bray, S.M.,Blackwood, J.K.,Kilkenny, M.L.,Coelho, M.A.,Foster, B.M.,Li, S.,Howard, J.A.,Pellegrini, L.,Albers, S.V.,Deery, M.J.,Robinson, N.P.
Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius.
Nat Commun, 6:8163-8163, 2015

PubMed Abstract: In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome for degradation. Recently, ubiquitin-like modifications have also been described in the archaeal domain of life. It has subsequently been hypothesized that ubiquitin-like proteasomal degradation might also operate in these microbes, since all archaeal species utilize homologues of the eukaryotic proteasome. Here we perform a structural and biochemical analysis of a ubiquitin-like modification pathway in the archaeon Sulfolobus acidocaldarius. We reveal that this modifier is homologous to the eukaryotic ubiquitin-related modifier Urm1, considered to be a close evolutionary relative of the progenitor of all ubiquitin-like proteins. Furthermore we demonstrate that urmylated substrates are recognized and processed by the archaeal proteasome, by virtue of a direct interaction with the modifier. Thus, the regulation of protein stability by Urm1 and the proteasome in archaea is likely representative of an ancient pathway from which eukaryotic ubiquitin-mediated proteolysis has evolved.

PubMed: 26348592
DOI: 10.1038/ncomms9163

Experimental method

X-RAY DIFFRACTION (2.2 Å)