Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RRH

The human prohibitin complex

Summary for 8RRH
Entry DOI10.2210/pdb8rrh/pdb
EMDB information19459
DescriptorProhibitin 1, Prohibitin-2 (2 entities in total)
Functional Keywordschaperone, lipid organization, protease regulator, membrane protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains11
Total formula weight345734.95
Authors
Lange, F.,Ratz, M.,Dohrke, J.N.,Wenzel, D.,Riedel, D.,Ilgen, P.,Jakobs, S. (deposition date: 2024-01-22, release date: 2024-12-18, Last modification date: 2025-04-02)
Primary citationLange, F.,Ratz, M.,Dohrke, J.N.,Le Vasseur, M.,Wenzel, D.,Ilgen, P.,Riedel, D.,Jakobs, S.
In situ architecture of the human prohibitin complex.
Nat.Cell Biol., 2025
Cited by
PubMed Abstract: Prohibitins are a highly conserved family of proteins that have been implicated in a variety of functions including mitochondrial stress signalling and housekeeping, cell cycle progression, apoptosis, lifespan regulation and many others. The human prohibitins prohibitin 1 and prohibitin 2 have been proposed to act as scaffolds within the mitochondrial inner membrane, but their molecular organization has remained elusive. Here we determined the molecular organization of the human prohibitin complex within the mitochondrial inner membrane using an integrative structural biology approach combining quantitative western blotting, cryo-electron tomography, subtomogram averaging and molecular modelling. The proposed bell-shaped structure consists of 11 alternating prohibitin 1 and prohibitin 2 molecules. This study reveals an average of about 43 prohibitin complexes per crista, covering 1-3% of the crista membrane area. These findings provide a structural basis for understanding the functional contributions of prohibitins to the integrity and spatial organization of the mitochondrial inner membrane.
PubMed: 40119201
DOI: 10.1038/s41556-025-01620-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (16.3 Å)
Structure validation

234785

PDB entries from 2025-04-16

PDB statisticsPDBj update infoContact PDBjnumon