#cparse("/super/config/super.config.vm") #cparse("${superIncludes}/super.before-doctype.fhtml") #cparse("${superIncludes}/super.legacy-doctype.fhtml") #cparse("${superIncludes}/super.head-top.fhtml") #cparse("/nsmb/includes/rj_global_meta_ft.fhtml") Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP - Nature Structural & Molecular Biology #cparse("/includes/foxtrot_adcode_vars.fhtml") #cparse("${superIncludes}/super.head-bottom.fhtml") #cparse("${superIncludes}/super.body-top.fhtml") #cparse("/nsmb/includes/rj_global_header_ft.fhtml")
 
#cparse("/nsmb/includes/rj_global_ltnav_ft.fhtml") #cparse("/nsmb/includes/rj_global_resources.fhtml") #cparse("/includes/npg_subject_area_subject_nav.html")
Article
Nature Structural Biology  6, 793 - 801 (1999)
doi:10.1038/11572
#cparse("//nsmb/journal/v6/n8/errorcorr/nsb0899_793_errcrr.fhtml")

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP

Douglas M. Freymann1, Robert J. Keenan2, Robert M. Stroud2 & Peter Walter2, 3

1  Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 E. Chicago Avenue, Chicago, Illinois 60611, USA.

2  Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143-0448, USA.

3  Howard Hughes Medical Institute, University of California, San Francisco, California 94143-0448, USA.

Correspondence should be addressed to Douglas M. Freymann freymann@nwu.edu
Ffh is a component of a bacterial ribonucleoprotein complex homologous to the signal recognition particle (SRP) of eukaryotes. It comprises three domains that mediate both binding to the hydrophobic signal sequence of the nascent polypeptide and the GTP-dependent interaction of Ffh with a structurally homologous GTPase of the SRP receptor. The X-ray structures of the two-domain 'NG' GTPase of Ffh in complex with Mg2+GDP and GDP have been determined at 2.0 Å resolution. The structures explain the low nucleotide affinity of Ffh and locate two regions of structural mobility at opposite sides of the nucleotide-binding site. One of these regions includes highly conserved sequence motifs that presumably contribute to the structural trigger signaling the GTP-bound state. The other includes the highly conserved interface between the N and G domains, and supports the hypothesis that the N domain regulates or signals the nucleotide occupancy of the G domain.

#cparse("/nsmb/journal/v6/n8/autonomy/embed/nsb0899_793.html")
 Top
Abstract
Previous
Table of contents
Full textFull text
Download PDFDownload PDF
Send to a friendSend to a friend
Save this linkSave this link
#cparse("/njobs/nsmb.html") #cparse("/includes/nature_products_box.fhtml") #cinclude("/nsmb/includes/rj_global_ad_sky_curr_back.fhtml")
Figures & Tables
Export citation
#cparse("/nsmb/includes/rj_global_footer_ft.fhtml")
 
Nature Publishing Group, publisher of Nature, and other science journals and reference works©1999 Nature Publishing Group | Privacy policy
#cinclude("/nsmb/includes/rj_global_ad_extra_article_back.fhtml") #cparse("${superIncludes}/super.body-bottom.fhtml")