2DX5

The complex structure between the mouse EAP45-GLUE domain and ubiquitin

Summary for 2DX5

• Entry DOI: 10.2210/pdb2dx5/pdb
• Descriptor: Vacuolar protein sorting protein 36, Ubiquitin (2 entities in total)
• Functional Keywords: ubiquitin, protein-protein complex, protein transport-signaling protein complex, protein transport/signaling protein
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm (By similarity): Q91XD6
• Total number of polymer chains: 2
• Total formula weight: 24645.16

Authors

Hirano, S.,Suzuki, N.,Slagsvold, T.,Kawasaki, M.,Trambaiolo, D.,Kato, R.,Stenmark, H.,Wakatsuki, S. (deposition date: 2006-08-24, release date: 2006-10-10, Last modification date: 2024-03-13)

Primary citation

Hirano, S.,Suzuki, N.,Slagsvold, T.,Kawasaki, M.,Trambaiolo, D.,Kato, R.,Stenmark, H.,Wakatsuki, S.
Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain
Nat.Struct.Mol.Biol., 13:1031-1032, 2006

PubMed Abstract: ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding.

PubMed: 17057714
DOI: 10.1038/nsmb1163

Experimental method

X-RAY DIFFRACTION (3.35 Å)