Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The prokaryotic origins of the COMMD protein family involved in eukaryotic membrane trafficking.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	May 29, 2026
Authors	Meihan Liu / Edmund R R Moody / Farrah Blades / Caroline Puente-Lelievre / Kai-En Chen / Ella J Stephens / Katharine A Michie / Rosemary J Cater / Tom A Williams / Brett M Collins / Michael D Healy /
PubMed Abstract	The ten eukaryotic COMMD proteins are core components of the Commander complex, with central roles in endosomal membrane trafficking and signalling. Each protein has an α-helical N-terminal (HN) ...The ten eukaryotic COMMD proteins are core components of the Commander complex, with central roles in endosomal membrane trafficking and signalling. Each protein has an α-helical N-terminal (HN) domain with a C-terminal copper metabolism gene MURR1 (COMM) domain. These ten family members assemble into a heterodecameric ring composed of five specific heterodimers. In this work we have combined structural homology searches with genome-wide predicted structures to identify ancestral COMMD-like proteins that exist as single genes in Bacteria and Archaea. Although there is limited sequence similarity to the eukaryotic proteins the bacterial and archaeal COMMD-like proteins are predicted to form homomeric ring-shaped assemblies like their eukaryotic counterparts. Our biophysical studies, crystal and cryo-EM structures confirm COMMD-like proteins readily form homooligomeric rings composed of eight or ten subunits assembled from core dimeric building blocks and inter-dimer interactions that are analogous to the heterodecameric core structure of the eukaryotic Commander complex. Phylogenetic analyses using amino acid sequences and FoldSeek structural alphabet (3Di) infer that the closest identified relatives to the eukaryotic COMMD proteins are found in Myxococcota bacteria. These findings indicate that COMMD genes emerged early in eukaryotic evolution through multiple rounds of duplication from a single ancestral gene likely acquired from bacteria.
External links	Nat Commun / PubMed:42215467
Methods	EM (single particle) / X-ray diffraction
Resolution	2.58 - 4.77 Å
Structure data	72266 9q6c EMDB-72266, PDB-9q6c: Cryo-EM structure of octameric COMMD-like protein MBK5214510 from Flavobacteriaceae bacterium Method: EM (single particle) / Resolution: 4.22 Å 72267 9q6d EMDB-72267, PDB-9q6d: CryoEM structure of decameric COMMD-like protein MBK5214510 from Flavobacteriaceae bacterium Method: EM (single particle) / Resolution: 4.77 Å 73963 9za1 EMDB-73963, PDB-9za1: cryoEM structure of COMMD-like protein S4Y171 octamer Method: EM (single particle) / Resolution: 3.4 Å 73964 9za2 EMDB-73964, PDB-9za2: cryoEM structure of COMMD-like protein S4Y171 octamer Method: EM (single particle) / Resolution: 4.7 Å PDB-9q6a: Crystal structure of octameric COMMD-like protein MBK5214510 from Flavobacteriaceae bacterium Method: X-RAY DIFFRACTION / Resolution: 2.58 Å
Chemicals	ChemComp-HOH: WATER
Source	flavobacteriaceae bacterium (bacteria) sorangium cellulosum so0157-2 (bacteria)
Keywords	UNKNOWN FUNCTION / COMMD / homooligomer / Commd-like / octamer / bacterial / Commander