1qzw
From Proteopedia
(New page: 200px<br /><applet load="1qzw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qzw, resolution 4.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1qzw.gif|left|200px]]<br /><applet load="1qzw" size=" | + | [[Image:1qzw.gif|left|200px]]<br /><applet load="1qzw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qzw, resolution 4.10Å" /> | caption="1qzw, resolution 4.10Å" /> | ||
'''Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication'''<br /> | '''Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Targeting of secretory and membrane proteins by the signal recognition | + | Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeon Sulfolobus solfataricus with and without its cognate SRP RNA binding site (helix 8) at 4-A resolution. The two structures show the flexibility of the SRP core and the position of SRP54 relative to the RNA. A long linker helix connects the GTPase (G domain) with the signal peptide binding (M) domain, and a hydrophobic contact between the N and M domains relates the signal peptide binding site to the G domain. Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome. |
==About this Structure== | ==About this Structure== | ||
| - | 1QZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http:// | + | 1QZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
[[Category: Montoya, G.]] | [[Category: Montoya, G.]] | ||
| - | [[Category: Rosendal, K | + | [[Category: Rosendal, K R.]] |
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: Wild, K.]] | [[Category: Wild, K.]] | ||
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[[Category: srp]] | [[Category: srp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:35 2008'' |
Revision as of 12:45, 21 February 2008
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Crystal structure of the complete core of archaeal SRP and implications for inter-domain communication
Overview
Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeon Sulfolobus solfataricus with and without its cognate SRP RNA binding site (helix 8) at 4-A resolution. The two structures show the flexibility of the SRP core and the position of SRP54 relative to the RNA. A long linker helix connects the GTPase (G domain) with the signal peptide binding (M) domain, and a hydrophobic contact between the N and M domains relates the signal peptide binding site to the G domain. Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome.
About this Structure
1QZW is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication., Rosendal KR, Wild K, Montoya G, Sinning I, Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14701-6. Epub 2003 Dec 1. PMID:14657338
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