3A4I

Crystal structure of GMP synthetase PH1347 from Pyrococcus horikoshii OT3

「2Z0C」から置き換えられました

3A4I の概要

• エントリーDOI: 10.2210/pdb3a4i/pdb
• 分子名称: GMP synthase [glutamine-hydrolyzing] subunit B (2 entities in total)
• 機能のキーワード: atp pyrophosphatase, glutamine amidotransferase, gmp synthetase, purine nucleotide biosynthesis, atp-binding, gmp biosynthesis, ligase, nucleotide-binding, purine biosynthesis
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69219.76

構造登録者

Maruoka, S.,Horita, S.,Lee, W.C.,Nagata, K.,Tanokura, M. (登録日: 2009-07-07, 公開日: 2009-07-21, 最終更新日: 2024-03-13)

主引用文献

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

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: 19900465
DOI: 10.1016/j.jmb.2009.10.053

実験手法

X-RAY DIFFRACTION (1.79 Å)