4wwm

X-ray crystal structure of Sulfolobus solfataricus Urm1

spinqualitylabelsall models 4wwm, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wwm is a 2 chain structure with sequence from Saccharolobus solfataricus 98/2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0KRX8_SACS9 Publication Abstract from PubMed 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. Involvement of a eukaryotic-like ubiquitin-related modifier in the proteasome pathway of the archaeon Sulfolobus acidocaldarius.,Anjum RS, Bray SM, Blackwood JK, Kilkenny ML, Coelho MA, Foster BM, Li S, Howard JA, Pellegrini L, Albers SV, Deery MJ, Robinson NP Nat Commun. 2015 Sep 8;6:8163. doi: 10.1038/ncomms9163. PMID:26348592 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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