8IGU
Hexameric Ring Complex of Engineered V1-ATPase: A3(De)3_empty
This is a non-PDB format compatible entry.
Replaces: 7COPSummary for 8IGU
Entry DOI | 10.2210/pdb8igu/pdb |
Related | 7COQ 8IGV 8IGW |
Descriptor | V-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B (3 entities in total) |
Functional Keywords | computational design, rotary molecular motor, complex, motor protein |
Biological source | Enterococcus hirae ATCC 9790 More |
Total number of polymer chains | 6 |
Total formula weight | 351230.30 |
Authors | Kosugi, T.,Tanabe, M.,Koga, N. (deposition date: 2023-02-21, release date: 2023-07-12, Last modification date: 2023-11-15) |
Primary citation | Kosugi, T.,Iida, T.,Tanabe, M.,Iino, R.,Koga, N. Design of allosteric sites into rotary motor V 1 -ATPase by restoring lost function of pseudo-active sites. Nat.Chem., 15:1591-1598, 2023 Cited by PubMed Abstract: Allostery produces concerted functions of protein complexes by orchestrating the cooperative work between the constituent subunits. Here we describe an approach to create artificial allosteric sites in protein complexes. Certain protein complexes contain subunits with pseudo-active sites, which are believed to have lost functions during evolution. Our hypothesis is that allosteric sites in such protein complexes can be created by restoring the lost functions of pseudo-active sites. We used computational design to restore the lost ATP-binding ability of the pseudo-active site in the B subunit of a rotary molecular motor, V-ATPase. Single-molecule experiments with X-ray crystallography analyses revealed that binding of ATP to the designed allosteric site boosts this V's activity compared with the wild-type, and the rotation rate can be tuned by modulating ATP's binding affinity. Pseudo-active sites are widespread in nature, and our approach shows promise as a means of programming allosteric control over concerted functions of protein complexes. PubMed: 37414880DOI: 10.1038/s41557-023-01256-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.77 Å) |
Structure validation
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