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

8IGU

Hexameric Ring Complex of Engineered V1-ATPase: A3(De)3_empty

This is a non-PDB format compatible entry.
Replaces:  7COP
Summary for 8IGU
Entry DOI10.2210/pdb8igu/pdb
Related7COQ 8IGV 8IGW
DescriptorV-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B (3 entities in total)
Functional Keywordscomputational design, rotary molecular motor, complex, motor protein
Biological sourceEnterococcus hirae ATCC 9790
More
Total number of polymer chains6
Total formula weight351230.30
Authors
Kosugi, T.,Tanabe, M.,Koga, N. (deposition date: 2023-02-21, release date: 2023-07-12, Last modification date: 2023-11-15)
Primary citationKosugi, 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: 37414880
DOI: 10.1038/s41557-023-01256-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.77 Å)
Structure validation

227561

건을2024-11-20부터공개중

PDB statisticsPDBj update infoContact PDBjnumon