1rj9: Difference between revisions

Revision as of 15:51, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1RJ9 is a Protein complex structure of sequences from Thermus aquaticus with and as ligands. 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 Thu Feb 21 14:51:24 2008

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OCA

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-[[Image:1rj9.gif|left|200px]]<br /><applet load="1rj9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rj9.gif|left|200px]]<br /><applet load="1rj9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rj9, resolution 1.9&Aring;" />
 '''Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)'''<br />
 ==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.
+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.
 ==About this Structure==
-RJ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG and GCP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJ9 OCA].
+RJ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GCP:'>GCP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJ9 OCA].
 ==Reference==
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 [[Category: Protein complex]]
 [[Category: Thermus aquaticus]]
-[[Category: Egea, P.F.]]
+[[Category: Egea, P F.]]
 [[Category: Napetschnig, J.]]
-[[Category: Savage, D.F.]]
+[[Category: Savage, D F.]]
-[[Category: Shan, S.O.]]
+[[Category: Shan, S O.]]
-[[Category: Stroud, R.M.]]
+[[Category: Stroud, R M.]]
 [[Category: Walter, P.]]
 [[Category: GCP]]
@@ Line 26: / Line 26: @@
 [[Category: srp-gtpase domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:38:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:24 2008''