5jne

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:42, 9 October 2024) (edit) (undo)
 
Line 9: Line 9:
</table>
</table>
== Function ==
== Function ==
-
[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.[https://www.uniprot.org/uniprot/SIZ1_YEAST SIZ1_YEAST] Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance.<ref>PMID:11572779</ref> <ref>PMID:11587849</ref> <ref>PMID:11333221</ref> <ref>PMID:11577116</ref> <ref>PMID:12226657</ref>
+
[https://www.uniprot.org/uniprot/UBC9_YEAST UBC9_YEAST] E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2).<ref>PMID:9341106</ref> <ref>PMID:11572779</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Post-translational protein modification by ubiquitin (Ub) and ubiquitin-like (Ubl) proteins such as small ubiquitin-like modifier (SUMO) regulates processes including protein homeostasis, the DNA damage response, and the cell cycle. Proliferating cell nuclear antigen (PCNA) is modified by Ub or poly-Ub at lysine (Lys)164 after DNA damage to recruit repair factors. Yeast PCNA is modified by SUMO on Lys164 and Lys127 during S-phase to recruit the anti-recombinogenic helicase Srs2. Lys164 modification requires specialized E2/E3 enzyme pairs for SUMO or Ub conjugation. For SUMO, Lys164 modification is strictly dependent on the E3 ligase Siz1, suggesting the E3 alters E2 specificity to promote Lys164 modification. The structural basis for substrate interactions in activated E3/E2-Ub/Ubl complexes remains unclear. Here we report an engineered E2 protein and cross-linking strategies that trap an E3/E2-Ubl/substrate complex for structure determination, illustrating how an E3 can bypass E2 specificity to force-feed a substrate lysine into the E2 active site.
 +
 
 +
Capturing a substrate in an activated RING E3/E2-SUMO complex.,Streich FC Jr, Lima CD Nature. 2016 Aug 18;536(7616):304-8. PMID:27509863<ref>PMID:27509863</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5jne" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==

Current revision

E2-SUMO-Siz1 E3-SUMO-PCNA complex

PDB ID 5jne

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools