Structural Insights into a New Homodimeric Self-activated GTPase Family

Overview

Journal EMBO Rep

Specialty Molecular Biology

Date 2007 May 1

PMID 17468740

Citations 21

Authors

Stephanie Gras

Valerie Chaumont

Bernard Fernandez

Philippe Carpentier

Fabienne Charrier-Savournin

Sophie Schmitt

Charles Pineau

Didier Flament

Arnaud Hecker

Patrick Forterre

Jean Armengaud

Dominique Housset

Affiliations

Soon will be listed here.

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.

Citing Articles

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