Summary for 3A4I
| Entry DOI | 10.2210/pdb3a4i/pdb |
| Descriptor | GMP synthase [glutamine-hydrolyzing] subunit B (2 entities in total) |
| Functional Keywords | atp pyrophosphatase, glutamine amidotransferase, gmp synthetase, purine nucleotide biosynthesis, atp-binding, gmp biosynthesis, ligase, nucleotide-binding, purine biosynthesis |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 2 |
| Total formula weight | 69219.76 |
| Authors | Maruoka, S.,Horita, S.,Lee, W.C.,Nagata, K.,Tanokura, M. (deposition date: 2009-07-07, release date: 2009-07-21, Last modification date: 2024-03-13) |
| Primary citation | Maruoka, S.,Horita, S.,Lee, W.C.,Nagata, K.,Tanokura, M. Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase Subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3. J.Mol.Biol., 395:417-429, 2010 Cited by PubMed Abstract: Guanosine 5'-monophosphate synthetase(s) (GMPS) catalyzes the final step of the de novo synthetic pathway of purine nucleotides. GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase (GATase) and ATP pyrophosphatase (ATPPase). GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl xanthosine 5'-monophosphate (adenyl-XMP) into guanosine 5'-monophosphate. Here we report the crystal structure of PH-ATPPase (the ATPPase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon Pyrococcus horikoshii OT3). PH-ATPPase consists of two domains (N-domain and C-domain) and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate (XMP)-binding site and also contributes to homodimerization. We have also demonstrated that PH-GATase (the glutamine amidotransferase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon P. horikoshii OT3) alone is inactive, and that all substrates of PH-ATPPase except for ammonia (Mg(2+), ATP and XMP) are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits. PubMed: 19900465DOI: 10.1016/j.jmb.2009.10.053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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