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8ORH

Knockout of GMC-oxidoreductase genes reveals that functional redundancy preserves mimivirus essential functions

Summary for 8ORH
Entry DOI10.2210/pdb8orh/pdb
EMDB information17125
DescriptorPutative GMC-type oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total)
Functional Keywordsgmc-oxidoreductase, genomic fiber, mimivirus, structural protein
Biological sourceMimivirus reunion
Total number of polymer chains2
Total formula weight155607.15
Authors
Primary citationAlempic, J.M.,Bisio, H.,Villalta, A.,Santini, S.,Lartigue, A.,Schmitt, A.,Bugnot, C.,Notaro, A.,Belmudes, L.,Adrait, A.,Poirot, O.,Ptchelkine, D.,De Castro, C.,Coute, Y.,Abergel, C.
Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes.
Microlife, 5:uqae006-uqae006, 2024
Cited by
PubMed Abstract: The mimivirus 1.2 Mb genome was shown to be organized into a nucleocapsid-like genomic fiber encased in the nucleoid compartment inside the icosahedral capsid. The genomic fiber protein shell is composed of a mixture of two GMC-oxidoreductase paralogs, one of them being the main component of the glycosylated layer of fibrils at the surface of the virion. In this study, we determined the effect of the deletion of each of the corresponding genes on the genomic fiber and the layer of surface fibrils. First, we deleted the GMC-oxidoreductase, the most abundant in the genomic fiber, and determined its structure and composition in the mutant. As expected, it was composed of the second GMC-oxidoreductase and contained 5- and 6-start helices similar to the wild-type fiber. This result led us to propose a model explaining their coexistence. Then we deleted the GMC-oxidoreductase, the most abundant in the layer of fibrils, to analyze its protein composition in the mutant. Second, we showed that the fitness of single mutants and the double mutant were not decreased compared with the wild-type viruses under laboratory conditions. Third, we determined that deleting the GMC-oxidoreductase genes did not impact the glycosylation or the glycan composition of the layer of surface fibrils, despite modifying their protein composition. Because the glycosylation machinery and glycan composition of members of different clades are different, we expanded the analysis of the protein composition of the layer of fibrils to members of the B and C clades and showed that it was different among the three clades and even among isolates within the same clade. Taken together, the results obtained on two distinct central processes (genome packaging and virion coating) illustrate an unexpected functional redundancy in members of the family , suggesting this may be the major evolutionary force behind their giant genomes.
PubMed: 38659623
DOI: 10.1093/femsml/uqae006
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.2 Å)
Structure validation

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건을2024-10-30부터공개중

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