1z43
From Proteopedia
(New page: 200px<br /><applet load="1z43" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z43, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1z43.gif|left|200px]]<br /><applet load="1z43" size=" | + | [[Image:1z43.gif|left|200px]]<br /><applet load="1z43" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z43, resolution 2.60Å" /> | caption="1z43, resolution 2.60Å" /> | ||
'''Crystal structure of 7S.S SRP RNA of M. jannaschii'''<br /> | '''Crystal structure of 7S.S SRP RNA of M. jannaschii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proper assembly of large protein-RNA complexes requires sequential binding | + | Proper assembly of large protein-RNA complexes requires sequential binding of the proteins to the RNA. The signal recognition particle (SRP) is a multiprotein-RNA complex responsible for the cotranslational targeting of proteins to biological membranes. Here we describe the crystal structure at 2.6-A resolution of the S-domain of SRP RNA from the archeon Methanococcus jannaschii. Comparison of this structure with the SRP19-bound form reveals the nature of the SRP19-induced conformational changes, which promote subsequent SRP54 attachment. These structural changes are initiated at the SRP19 binding site and transmitted through helix 6 to looped-out adenosines, which form tertiary RNA interaction with helix 8. Displacement of these adenosines enforces a conformational change of the asymmetric loop structure in helix 8. In free RNA, the three unpaired bases A195, C196, and C197 are directed toward the helical axis, whereas upon SRP19 binding the loop backbone inverts and the bases are splayed out in a conformation that resembles the SRP54-bound form. Nucleotides adjacent to the bulged nucleotides seem to be particularly important in the regulation of this loop transition. Binding of SRP19 to 7S RNA reveals an elegant mechanism of how protein-induced changes are directed through an RNA molecule and may relate to those regulating the assembly of other RNPs. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z43 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1Z43 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z43 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hainzl, T.]] | [[Category: Hainzl, T.]] | ||
[[Category: Huang, S.]] | [[Category: Huang, S.]] | ||
| - | [[Category: Sauer-Eriksson, A | + | [[Category: Sauer-Eriksson, A E.]] |
[[Category: rna]] | [[Category: rna]] | ||
[[Category: tetra-loop]] | [[Category: tetra-loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:00 2008'' |
Revision as of 14:12, 21 February 2008
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Crystal structure of 7S.S SRP RNA of M. jannaschii
Overview
Proper assembly of large protein-RNA complexes requires sequential binding of the proteins to the RNA. The signal recognition particle (SRP) is a multiprotein-RNA complex responsible for the cotranslational targeting of proteins to biological membranes. Here we describe the crystal structure at 2.6-A resolution of the S-domain of SRP RNA from the archeon Methanococcus jannaschii. Comparison of this structure with the SRP19-bound form reveals the nature of the SRP19-induced conformational changes, which promote subsequent SRP54 attachment. These structural changes are initiated at the SRP19 binding site and transmitted through helix 6 to looped-out adenosines, which form tertiary RNA interaction with helix 8. Displacement of these adenosines enforces a conformational change of the asymmetric loop structure in helix 8. In free RNA, the three unpaired bases A195, C196, and C197 are directed toward the helical axis, whereas upon SRP19 binding the loop backbone inverts and the bases are splayed out in a conformation that resembles the SRP54-bound form. Nucleotides adjacent to the bulged nucleotides seem to be particularly important in the regulation of this loop transition. Binding of SRP19 to 7S RNA reveals an elegant mechanism of how protein-induced changes are directed through an RNA molecule and may relate to those regulating the assembly of other RNPs.
About this Structure
1Z43 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structural insights into SRP RNA: an induced fit mechanism for SRP assembly., Hainzl T, Huang S, Sauer-Eriksson AE, RNA. 2005 Jul;11(7):1043-50. Epub 2005 May 31. PMID:15928341
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