2UYZ

Non-covalent complex between Ubc9 and SUMO1

Summary for 2UYZ

• Entry DOI: 10.2210/pdb2uyz/pdb
• Related: 1A5R 1TGZ 1U9A 1U9B 1WYW 1Y8R 1Z5S 2ASQ 2BF8 2G4D 2IO2 2IY0 2IY1
• Descriptor: SUMO-CONJUGATING ENZYME UBC9, SMALL UBIQUITIN-RELATED MODIFIER 1, SODIUM ION, ... (4 entities in total)
• Functional Keywords: sumoylation, cell division, nuclear protein, ubiquitin-like modifier, ubl conjugation pathway, conjugating enzyme, chromosome partition, e2, ubc9, sumo1, ligase, mitosis, cell cycle
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Nucleus: P63280; Nucleus membrane: P63165
• Total number of polymer chains: 2
• Total formula weight: 27268.30

Authors

Knipscheer, P.,van Dijk, W.J.,Olsen, J.V.,Mann, M.,Sixma, T.K. (deposition date: 2007-04-21, release date: 2007-06-12, Last modification date: 2023-12-13)

Primary citation

Knipscheer, P.,van Dijk, W.J.,Olsen, J.V.,Mann, M.,Sixma, T.K.
Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation.
EMBO J., 26:2797-2807, 2007

PubMed Abstract: The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.

PubMed: 17491593
DOI: 10.1038/sj.emboj.7601711

Experimental method

X-RAY DIFFRACTION (1.4 Å)