1ng1: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1ng1.jpg|left|200px]] | [[Image:1ng1.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1ng1", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1ng1| PDB=1ng1 | SCENE= }} | |||
}} | |||
'''N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS''' | '''N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS''' | ||
Line 28: | Line 25: | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
[[Category: Walter, P.]] | [[Category: Walter, P.]] | ||
[[Category: | [[Category: Ffh]] | ||
[[Category: | [[Category: Gdp]] | ||
[[Category: | [[Category: Gtpase]] | ||
[[Category: | [[Category: Mg]] | ||
[[Category: | [[Category: Signal recognition particle]] | ||
[[Category: | [[Category: Srp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:29:21 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 02:29, 3 May 2008
N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
OverviewOverview
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.
About this StructureAbout this Structure
1NG1 is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
ReferenceReference
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP., Freymann DM, Keenan RJ, Stroud RM, Walter P, Nat Struct Biol. 1999 Aug;6(8):793-801. PMID:10426959 Page seeded by OCA on Sat May 3 02:29:21 2008