Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP - PubMed (original) (raw)
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP
D M Freymann et al. Nat Struct Biol. 1999 Aug.
Abstract
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 A 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.
Similar articles
- Structure of the conserved GTPase domain of the signal recognition particle.
Freymann DM, Keenan RJ, Stroud RM, Walter P. Freymann DM, et al. Nature. 1997 Jan 23;385(6614):361-4. doi: 10.1038/385361a0. Nature. 1997. PMID: 9002524 - Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
Montoya G, Svensson C, Luirink J, Sinning I. Montoya G, et al. Nature. 1997 Jan 23;385(6614):365-8. doi: 10.1038/385365a0. Nature. 1997. PMID: 9002525 - Interaction of guanine nucleotides with the signal recognition particle from Escherichia coli.
Jagath JR, Rodnina MV, Lentzen G, Wintermeyer W. Jagath JR, et al. Biochemistry. 1998 Nov 3;37(44):15408-13. doi: 10.1021/bi981523a. Biochemistry. 1998. PMID: 9799502 - The guanine nucleotide-binding switch in three dimensions.
Vetter IR, Wittinghofer A. Vetter IR, et al. Science. 2001 Nov 9;294(5545):1299-304. doi: 10.1126/science.1062023. Science. 2001. PMID: 11701921 Review. - GEF-mediated GDP/GTP exchange by monomeric GTPases: a regulatory role for Mg2+?
Pan JY, Wessling-Resnick M. Pan JY, et al. Bioessays. 1998 Jun;20(6):516-21. doi: 10.1002/(SICI)1521-1878(199806)20:6<516::AID-BIES11>3.0.CO;2-3. Bioessays. 1998. PMID: 9699463 Review.
Cited by
- Structure of the GDP-bound state of the SRP GTPase FlhF.
Dornes A, Mais CN, Bange G. Dornes A, et al. Acta Crystallogr F Struct Biol Commun. 2024 Mar 1;80(Pt 3):53-58. doi: 10.1107/S2053230X24000979. Epub 2024 Feb 20. Acta Crystallogr F Struct Biol Commun. 2024. PMID: 38376823 Free PMC article. - Molecular basis and current insights of atypical Rho small GTPase in cancer.
Huang H, Wang S, Guan Y, Ren J, Liu X. Huang H, et al. Mol Biol Rep. 2024 Jan 18;51(1):141. doi: 10.1007/s11033-023-09140-7. Mol Biol Rep. 2024. PMID: 38236467 Review. - Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.
Czech L, Mais CN, Kratzat H, Sarmah P, Giammarinaro P, Freibert SA, Esser HF, Musial J, Berninghausen O, Steinchen W, Beckmann R, Koch HG, Bange G. Czech L, et al. Nat Commun. 2022 Feb 25;13(1):1069. doi: 10.1038/s41467-022-28675-0. Nat Commun. 2022. PMID: 35217658 Free PMC article. - The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.
Ford MGJ, Chappie JS. Ford MGJ, et al. Traffic. 2019 Oct;20(10):717-740. doi: 10.1111/tra.12676. Epub 2019 Aug 26. Traffic. 2019. PMID: 31298797 Free PMC article. Review. - ATPase and GTPase Tangos Drive Intracellular Protein Transport.
Shan SO. Shan SO. Trends Biochem Sci. 2016 Dec;41(12):1050-1060. doi: 10.1016/j.tibs.2016.08.012. Epub 2016 Sep 19. Trends Biochem Sci. 2016. PMID: 27658684 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Molecular Biology Databases