1rj9: Difference between revisions

Revision as of 14:55, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rj9.png

Template:STRUCTURE 1rj9

Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)

Template:ABSTRACT PUBMED 14724630

About this StructureAbout this Structure

1RJ9 is a Protein complex structure of sequences from Thermus aquaticus. Full crystallographic information is available from OCA.

ReferenceReference

Substrate twinning activates the signal recognition particle and its receptor., Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM, Nature. 2004 Jan 15;427(6971):215-21. PMID:14724630

Page seeded by OCA on Mon Jul 28 14:55:50 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1rj9|  PDB=1rj9  |  SCENE=  }}
-'''Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)'''
+===Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)===
-==Overview==
+<!--
-Signal sequences target proteins for secretion from cells or for integration into cell membranes. As nascent proteins emerge from the ribosome, signal sequences are recognized by the signal recognition particle (SRP), which subsequently associates with its receptor (SR). In this complex, the SRP and SR stimulate each other's GTPase activity, and GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane. To define the mechanism of reciprocal activation, we determined the 1.9 A structure of the complex formed between these two GTPases. The two partners form a quasi-two-fold symmetrical heterodimer. Biochemical analysis supports the importance of the extensive interaction surface. Complex formation aligns the two GTP molecules in a symmetrical, composite active site, and the 3'OH groups are essential for association, reciprocal activation and catalysis. This unique circle of twinned interactions is severed twice on hydrolysis, leading to complex dissociation after cargo delivery.
+The line below this paragraph, {{ABSTRACT_PUBMED_14724630}}, adds the Publication Abstract to the page
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 [[Category: Protein-protein complex]]
 [[Category: Srp-gtpase domain]]
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