2ged: Difference between revisions

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[[Image:2ged.gif|left|200px]]
[[Image:2ged.gif|left|200px]]


{{Structure
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|GENE= SRP102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ged FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ged OCA], [http://www.ebi.ac.uk/pdbsum/2ged PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ged RCSB]</span>
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'''Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form'''
'''Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form'''
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[[Category: Schmidt, D.]]
[[Category: Schmidt, D.]]
[[Category: Schwartz, T U.]]
[[Category: Schwartz, T U.]]
[[Category: circular permutation]]
[[Category: Circular permutation]]
[[Category: g protein]]
[[Category: G protein]]
[[Category: proline isomerization]]
[[Category: Proline isomerization]]
[[Category: protein transport]]
[[Category: Protein transport]]
[[Category: signal recognition particle]]
[[Category: Signal recognition particle]]
 
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Revision as of 05:00, 4 May 2008

File:2ged.gif

Template:STRUCTURE 2ged

Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form


OverviewOverview

Protein translocation across and insertion into membranes is essential to all life forms. Signal peptide-bearing nascent polypeptide chains emerging from the ribosome are first sampled by the signal-recognition particle (SRP), then targeted to the membrane via the SRP receptor (SR), and, finally, transferred to the protein-conducting channel. In eukaryotes, this process is tightly controlled by the concerted action of three G proteins, the 54-kD subunit of SRP and the alpha- and beta-subunits of SR. We have determined the 2.2-A crystal structure of the nucleotide-free SRbeta domain. Unexpectedly, the structure is a homodimer with a highly intertwined interface made up of residues from the switch regions of the G domain. The remodeling of the switch regions does not resemble any of the known G protein switch mechanisms. Biochemical analysis confirms homodimerization in vitro, which is incompatible with SRalpha binding. The switch mechanism involves cis/trans isomerization of a strictly conserved proline, potentially implying a new layer of regulation of cotranslational transport.

About this StructureAbout this Structure

2GED is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region., Schwartz TU, Schmidt D, Brohawn SG, Blobel G, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6823-8. Epub 2006 Apr 20. PMID:16627619 Page seeded by OCA on Sun May 4 05:00:37 2008

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