2ged
From Proteopedia
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| - | [[Image:2ged.gif|left|200px]] | + | [[Image:2ged.gif|left|200px]] |
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| - | '''Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form''' | + | {{Structure |
| + | |PDB= 2ged |SIZE=350|CAPTION= <scene name='initialview01'>2ged</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= SRP102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GED is a [ | + | 2GED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GED OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16627619 16627619] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal recognition particle]] | [[Category: signal recognition particle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:03:42 2008'' |
Revision as of 15:03, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SRP102 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Signal Recognition Particle Receptor Beta-Subunit in nucleotide-free dimerized form
Overview
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 Structure
2GED is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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