2VRR

Structure of SUMO modified Ubc9

Summary for 2VRR

• Entry DOI: 10.2210/pdb2vrr/pdb
• Related: 1A5R 1TGZ 1U9A 1U9B 1WYW 1Y8R 1Z5S 2ASQ 2BF8 2IO2 2IY0 2IY1 2UYZ
• Descriptor: SUMO-CONJUGATING ENZYME UBC9, SMALL UBIQUITIN-RELATED MODIFIER 1, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: e2, ubc9, sumo, ligase, nucleus, mitosis, membrane, phosphoprotein, isopeptide bond, chromosome partition, posttranslational modification, ubl conjugation pathway, ubiquitin like molecule, developmental protein, host-virus interaction, cytoplasm, cell cycle, modification, cell division, cell cycle/ligase, cell cycle-ligase complex
• Biological source: MUS MUSCULUS (MOUSE); More
• Total number of polymer chains: 2
• Total formula weight: 27468.46

Authors

Knipscheer, P.,Flotho, A.,Klug, H.,Olsen, J.V.,van Dijk, W.J.,Fish, A.,Johnson, E.S.,Mann, M.,Sixma, T.K.,Pichler, A. (deposition date: 2008-04-13, release date: 2008-08-19, Last modification date: 2023-12-13)

Primary citation

Knipscheer, P.,Flotho, A.,Klug, H.,Olsen, J.V.,van Dijk, W.J.,Fish, A.,Johnson, E.S.,Mann, M.,Sixma, T.K.,Pichler, A.
Ubc9 sumoylation regulates SUMO target discrimination.
Mol. Cell, 31:371-382, 2008

PubMed Abstract: Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.

PubMed: 18691969
DOI: 10.1016/j.molcel.2008.05.022

Experimental method

X-RAY DIFFRACTION (2.22 Å)