3EAB

Crystal structure of Spastin MIT in complex with ESCRT III

Summary for 3EAB

• Entry DOI: 10.2210/pdb3eab/pdb
• Descriptor: Spastin, CHMP1b (2 entities in total)
• Functional Keywords: spastin, chmp, mit, escrt, alternative splicing, atp-binding, cytoplasm, disease mutation, hereditary spastic paraplegia, nucleotide-binding, nucleus, polymorphism, cell cycle
• Biological source: Homo sapiens (Human); More
• Cellular location: Membrane; Single-pass membrane protein (Potential): Q9UBP0
• Total number of polymer chains: 12
• Total formula weight: 94415.32

Authors

Yang, D.,Rimanchi, N.,Renvoise, B.,Lippincott-Schwartz, J.,Blackstone, C.,Hurley, J.H. (deposition date: 2008-08-25, release date: 2008-11-11, Last modification date: 2024-02-21)

Primary citation

Yang, D.,Rismanchi, N.,Renvoise, B.,Lippincott-Schwartz, J.,Blackstone, C.,Hurley, J.H.
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B.
Nat.Struct.Mol.Biol., 15:1278-1286, 2008

PubMed Abstract: The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT-III, localizes to the midbody and participates in the membrane-abscission step of cytokinesis. The ESCRT-III protein charged multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT domain-containing protein spastin, a microtubule-severing enzyme, to the midbody. The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4-CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen-bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT-III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis.

PubMed: 18997780
DOI: 10.1038/nsmb.1512

Experimental method

X-RAY DIFFRACTION (2.5 Å)