1YR9

PAB0955 crystal structure : a GTPase in GDP and PO4 bound form from Pyrococcus abyssi

1YR9 の概要

• エントリーDOI: 10.2210/pdb1yr9/pdb
• 関連するPDBエントリー: 1YR6 1YR7 1YR8 1YRA 1YRB
• 分子名称: ATP(GTP)binding protein, PHOSPHATE ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gtp binding protein, gtpase, p-loop, rossmann fold, gdp, hydrolase
• 由来する生物種: Pyrococcus abyssi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30872.97

構造登録者

Gras, S.,Carpentier, P.,Armengaud, J.,Housset, D. (登録日: 2005-02-03, 公開日: 2006-02-14, 最終更新日: 2023-10-25)

主引用文献

Gras, S.,Chaumont, V.,Fernandez, B.,Carpentier, P.,Charrier-Savournin, F.,Schmitt, S.,Pineau, C.,Flament, D.,Hecker, A.,Forterre, P.,Armengaud, J.,Housset, D.
Structural insights into a new homodimeric self-activated GTPase family.
Embo Rep., 8:569-575, 2007

PubMed Abstract: The human XAB1/MBDin GTPase and its close homologues form one of the ten phylogenetically distinct families of the SIMIBI (after signal recognition particle, MinD and BioD) class of phosphate-binding loop NTPases. The genomic context and the partners identified for the archaeal and eukaryotic homologues indicate that they are involved in genome maintenance--DNA repair or replication. The crystal structure of PAB0955 from Pyrococcus abyssi shows that, unlike other SIMIBI class G proteins, these highly conserved GTPases are homodimeric, regardless of the presence of nucleotides. The nucleotide-binding site of PAB0955 is rather rigid and its conformation is closest to that of the activated SRP G domain. One insertion to the G domain bears a strictly conserved GPN motif, which is part of the catalytic site of the other monomer and stabilizes the phosphate ion formed. Owing to this unique functional feature, we propose to call this family as GPN-loop GTPase.

PubMed: 17468740
DOI: 10.1038/sj.embor.7400958

実験手法

X-RAY DIFFRACTION (2.8 Å)