3E1R

Midbody targeting of the ESCRT machinery by a non-canonical coiled-coil in CEP55

Summary for 3E1R

• Entry DOI: 10.2210/pdb3e1r/pdb
• Descriptor: Centrosomal protein of 55 kDa, Programmed cell death 6-interacting protein (3 entities in total)
• Functional Keywords: cep55, alix, cytokinesis, escrt, alternative splicing, cell cycle, cell division, coiled coil, mitosis, phosphoprotein, polymorphism, acetylation, apoptosis, cytoplasm, host-virus interaction, protein transport, transport, cell cycle-transport protein complex, cell cycle/transport protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole: Q53EZ4; Cytoplasm, cytosol: Q8WUM4
• Total number of polymer chains: 3
• Total formula weight: 15118.05

Authors

Lee, H.H.,Elia, N.,Ghirlando, R.,Lippincott-Schwartz, J.,Hurley, J.H. (deposition date: 2008-08-04, release date: 2008-11-04, Last modification date: 2024-02-21)

Primary citation

Lee, H.H.,Elia, N.,Ghirlando, R.,Lippincott-Schwartz, J.,Hurley, J.H.
Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55.
Science, 322:576-580, 2008

PubMed Abstract: The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT and ALIX-binding region (EABR) of CEP55. We solved the crystal structure of EABR bound to an ALIX peptide at a resolution of 2.0 angstroms. The structure shows that EABR forms an aberrant dimeric parallel coiled coil. Bulky and charged residues at the interface of the two central heptad repeats create asymmetry and a single binding site for an ALIX or TSG101 peptide. Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function.

PubMed: 18948538
DOI: 10.1126/science.1162042

Experimental method

X-RAY DIFFRACTION (2 Å)