6IQE

Human prohibitin 2

Summary for 6IQE

• Entry DOI: 10.2210/pdb6iqe/pdb
• Descriptor: Prohibitin-2 (2 entities in total)
• Functional Keywords: mitochondrial function and morphology, transcriptional modulation, coiled coil, protein binding
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 9818.11

Authors

Hirano, Y.,Koshiba, T.,Tamada, T. (deposition date: 2018-11-07, release date: 2019-09-25, Last modification date: 2023-11-22)

Primary citation

Yoshinaka, T.,Kosako, H.,Yoshizumi, T.,Furukawa, R.,Hirano, Y.,Kuge, O.,Tamada, T.,Koshiba, T.
Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region.
Iscience, 19:1065-1078, 2019

PubMed Abstract: The coiled-coil motif mediates subunit oligomerization and scaffolding and underlies several fundamental biologic processes. Prohibitins (PHBs), mitochondrial inner membrane proteins involved in mitochondrial homeostasis and signal transduction, are predicted to have a coiled-coil motif, but their structural features are poorly understood. Here we solved the crystal structure of the heptad repeat (HR) region of PHB2 at 1.7-Å resolution, showing that it assembles into a dimeric, antiparallel coiled-coil with a unique negatively charged area essential for the PHB interactome in mitochondria. Disruption of the HR coiled-coil abolishes well-ordered PHB complexes and the mitochondrial tubular networks accompanying PHB-dependent signaling. Using a proximity-dependent biotin identification (BioID) technique in live cells, we mapped a number of mitochondrial intermembrane space proteins whose association with PHB2 relies on the HR coiled-coil region. Elucidation of the PHB complex structure in mitochondria provides insight into essential PHB interactomes required for mitochondrial dynamics as well as signal transduction.

PubMed: 31522117
DOI: 10.1016/j.isci.2019.08.056

Experimental method

X-RAY DIFFRACTION (1.701 Å)