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Structural insights into a new homodimeric self-activated GTPase family
Provedor de dados: 5
Autores: Gras, S; Chaumont, V; Fernandez, B; Carpentier, P; Charrier Savournin, F; Schmitt, Sophie; Pineau, C; Flament, Didier; Hecker, A; Forterre, P; Armengaud, J; Housset, D.
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...
Tipo: Text
Palavras-chave: Structure; SIMIBI; Replication; GTPase; Crystal.
Ano: 2007
URL: http://archimer.ifremer.fr/doc/2007/publication-4724.pdf