3GGZ: Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif

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.
PDB ID: 3GGZDownload
MMDB ID: 76568
PDB Deposition Date: 2009/3/2
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 3.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3GGZ: dimeric; determined by author and by software (PISA)
Molecular Components in 3GGZ
Label Count Molecule
Proteins (2 molecules)
Increased Sodium Tolerance Protein 1(Gene symbol: IST1)
Molecule annotation
Vacuolar Protein-sorting-associated Protein 46(Gene symbol: DID2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB