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SUMO

From Proteopedia

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Line 35: Line 35:
**[[2n1w]], [[5ghb]], [[5ghc]] – hSUMO-2 - NMR<br />
**[[2n1w]], [[5ghb]], [[5ghc]] – hSUMO-2 - NMR<br />
**[[1u4a]] – hSUMO-3 (mutant) – NMR <br />
**[[1u4a]] – hSUMO-3 (mutant) – NMR <br />
 +
**[[5xqm]] – SUMO-1 - ''Caenorhabditis elegans'' - NMR<br />
* SUMO+ubiquitin-like SUMO-conjugating enzyme
* SUMO+ubiquitin-like SUMO-conjugating enzyme
Line 61: Line 62:
**[[2bf8]] - SUMO-1+E2 - bovine<br />
**[[2bf8]] - SUMO-1+E2 - bovine<br />
-
* SMT3
+
* SMT3 or ubiquitin-like protein Smt3
-
**[[2k1f]] – SMT3 – Fruit fly<br />
+
**[[2k1f]] – SMT3 – ''Drosophila melanogaster''<br />
-
**[[2eke]] – ySMT3+UBC9 – yeast<br />
+
**[[1l2n]] – ySMT3 – yeast - NMR<br />
 +
**[[2eke]] – ySMT3+UBC9 <br />
**[[1euv]] – ySMT3+ULP1 protease<br />
**[[1euv]] – ySMT3+ULP1 protease<br />
**[[3v60]], [[3v61]] – ySMT3 + PCNA (mutant)<br />
**[[3v60]], [[3v61]] – ySMT3 + PCNA (mutant)<br />
**[[3v62]] – ySMT3 + PCNA (mutant) + ATP-dependent DNA helicase SRS2<br />
**[[3v62]] – ySMT3 + PCNA (mutant) + ATP-dependent DNA helicase SRS2<br />
**[[3qht]] – ySMT3 + monobody<br />
**[[3qht]] – ySMT3 + monobody<br />
 +
**[[2io1]] – hSMT3 + Senp2<br />
 +
**[[2mp2]] – hSMT3 + RNF4<br />
* SUMO+other proteins
* SUMO+other proteins

Revision as of 21:24, 21 September 2018

Human SUMO-1 (yellow) complex with SUMO-activating enzyme subunit 1 (grey), SUMO-activating enzyme subunit 2 (green), adenosine derivative and Zn+2 ion (grey) (PDB code 3kyc)

Drag the structure with the mouse to rotate

3D Structures of SUMO

Updated on 21-September-2018

Reference

  1. ↑ Sarge KD, Park-Sarge OK. Sumoylation and human disease pathogenesis. Trends Biochem Sci. 2009 Apr;34(4):200-5. doi: 10.1016/j.tibs.2009.01.004. Epub, 2009 Mar 11. PMID:19282183 doi:http://dx.doi.org/10.1016/j.tibs.2009.01.004
  2. ↑ Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 2010 Feb 18;463(7283):906-12. PMID:20164921 doi:10.1038/nature08765

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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