5X09
Crystal structure of subunit A mutant P235A/S238C of the A-ATP synthase from pyrococcus horikoshii OT3
Summary for 5X09
| Entry DOI | 10.2210/pdb5x09/pdb |
| Descriptor | V-type ATP synthase alpha chain,V-type ATP synthase alpha chain, ACETIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
| Functional Keywords | p loop, proline mutant, serine mutant, hydrolase |
| Biological source | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) More |
| Total number of polymer chains | 1 |
| Total formula weight | 60813.76 |
| Authors | Dhirendra, S.,Gruber, G. (deposition date: 2017-01-20, release date: 2017-11-29, Last modification date: 2023-11-22) |
| Primary citation | Singh, D.,Gruber, G. Crystallographic and enzymatic insights into the mechanisms of Mg-ADP inhibition in the A1 complex of the A1AO ATP synthase J. Struct. Biol., 201:26-35, 2018 Cited by PubMed Abstract: F-ATP synthases are described to have mechanisms which regulate the unnecessary depletion of ATP pool during an energy limited state of the cell. Mg-ADP inhibition is one of the regulatory features where Mg-ADP gets entrapped in the catalytic site, preventing the binding of ATP and further inhibiting ATP hydrolysis. Knowledge about the existence and regulation of the related archaeal-type AA ATP synthases (ABCDEFGac) is limited. We demonstrate MgADP inhibition of the enzymatically active ABD- and ABDF complexes of Methanosarcina mazei Gö1 A-ATP synthase and reveal the importance of the amino acids P235 and S238 inside the P-loop (GPFGSGKTV) of the catalytic A subunit. Substituting these two residues by the respective P-loop residues alanine and cysteine (GAFGCGKTV) of the related eukaryotic V-ATPase increases significantly the ATPase activity of the enzyme variant and abolishes MgADP inhibition. The atomic structure of the P235A, S238C double mutant of subunit A of the Pyrococcus horikoshii OT3 A-ATP synthase provides details of how these critical residues affect nucleotide-binding and ATP hydrolysis in this molecular engine. The qualitative data are confirmed by quantitative results derived from fluorescence correlation spectroscopy experiments. PubMed: 29074108DOI: 10.1016/j.jsb.2017.10.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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