3GGZ

Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif

Summary for 3GGZ

• Entry DOI: 10.2210/pdb3ggz/pdb
• Related: 3GGY
• Descriptor: Increased sodium tolerance protein 1, Vacuolar protein-sorting-associated protein 46 (2 entities in total)
• Functional Keywords: novel mim binding mode, phosphoprotein, coiled coil, endosome, membrane, protein transport, transport, endocytosis
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Cytoplasm: P53843; Endosome membrane; Peripheral membrane protein: P69771
• Total number of polymer chains: 8
• Total formula weight: 102887.83

Authors

Xiao, J.,Xu, Z. (deposition date: 2009-03-02, release date: 2009-09-08, Last modification date: 2024-02-21)

Primary citation

Xiao, J.,Chen, X.W.,Davies, B.A.,Saltiel, A.R.,Katzmann, D.J.,Xu, Z.
Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis.
MOLECULAR BIOLOGY OF THE CELL, 20:3514-3524, 2009

PubMed Abstract: The ESCRT machinery functions in several important eukaryotic cellular processes. The AAA-ATPase Vps4 catalyzes disassembly of the ESCRT-III complex and may regulate membrane deformation and vesicle scission as well. Ist1 was proposed to be a regulator of Vps4, but its mechanism of action was unclear. The crystal structure of the N-terminal domain of Ist1 (Ist1NTD) reveals an ESCRT-III subunit-like fold, implicating Ist1 as a divergent ESCRT-III family member. Ist1NTD specifically binds to the ESCRT-III subunit Did2, and cocrystallization of Ist1NTD with a Did2 fragment shows that Ist1 interacts with the Did2 C-terminal MIM1 (MIT-interacting motif 1) via a novel MIM-binding structural motif. This arrangement indicates a mechanism for intermolecular ESCRT-III subunit association and may also suggest one form of ESCRT-III subunit autoinhibition via intramolecular interaction.

PubMed: 19477918
DOI: 10.1091/mbc.E09-05-0403

Experimental method

X-RAY DIFFRACTION (3.8 Å)