6H9M

Coiled-coil domain-containing protein 90B residues 43-125 from Homo sapiens fused to a GCN4 adaptor

Summary for 6H9M

• Entry DOI: 10.2210/pdb6h9m/pdb
• Descriptor: Coiled-coil domain-containing protein 90B, mitochondrial,General control protein GCN4 (2 entities in total)
• Functional Keywords: coiled coil, beta-layer, mitochondrial membrane, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 40708.54

Authors

Adlakha, J.,Albrecht, R.,Lupas, A.N.,Hernandez Alvarez, B.,Hartmann, M.D. (deposition date: 2018-08-04, release date: 2019-02-13, Last modification date: 2024-01-17)

Primary citation

Adlakha, J.,Karamichali, I.,Sangwallek, J.,Deiss, S.,Bar, K.,Coles, M.,Hartmann, M.D.,Lupas, A.N.,Hernandez Alvarez, B.
Characterization of MCU-Binding Proteins MCUR1 and CCDC90B - Representatives of a Protein Family Conserved in Prokaryotes and Eukaryotic Organelles.
Structure, 27:464-475.e6, 2019

PubMed Abstract: Membrane-bound coiled-coil proteins are important mediators of signaling, fusion, and scaffolding. Here, we delineate a heterogeneous group of trimeric membrane-anchored proteins in prokaryotes and eukaryotic organelles with a characteristic head-neck-stalk-anchor architecture, in which a membrane-anchored coiled-coil stalk projects an N-terminal head domain via a β-layer neck. Based on sequence analysis, we identify different types of head domains and determine crystal structures of two representatives, the archaeal protein Kcr-0859 and the human CCDC90B, which possesses the most widespread head type. Using mitochondrial calcium uniporter regulator 1 (MCUR1), the functionally characterized paralog of CCDC90B, we study the role of individual domains, and find that the head interacts directly with the mitochondrial calcium uniporter (MCU) and is destabilized upon Ca binding. Our data provide structural details of a class of membrane-bound coiled-coil proteins and identify the conserved head domain of the most widespread type as a mediator of their function.

PubMed: 30612859
DOI: 10.1016/j.str.2018.11.004

Experimental method

X-RAY DIFFRACTION (2.1 Å)