1lng
From Proteopedia
(New page: 200px<br /><applet load="1lng" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lng, resolution 2.3Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1lng.gif|left|200px]]<br /><applet load="1lng" size=" | + | [[Image:1lng.gif|left|200px]]<br /><applet load="1lng" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lng, resolution 2.3Å" /> | caption="1lng, resolution 2.3Å" /> | ||
'''Crystal Structure of the SRP19-7S.S SRP RNA Complex of M. jannaschii'''<br /> | '''Crystal Structure of the SRP19-7S.S SRP RNA Complex of M. jannaschii'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The signal recognition particle (SRP) is a phylogenetically conserved | + | The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein. It associates with ribosomes to mediate co-translational targeting of membrane and secretory proteins to biological membranes. In mammalian cells, the SRP consists of a 7S RNA and six protein components. The S domain of SRP comprises the 7S.S part of RNA bound to SRP19, SRP54 and the SRP68/72 heterodimer; SRP54 has the main role in recognizing signal sequences of nascent polypeptide chains and docking SRP to its receptor. During assembly of the SRP, binding of SRP19 precedes and promotes the association of SRP54 (refs 4, 5). Here we report the crystal structure at 2.3 A resolution of the complex formed between 7S.S RNA and SRP19 in the archaeon Methanococcus jannaschii. SRP19 bridges the tips of helices 6 and 8 of 7S.S RNA by forming an extensive network of direct protein RNA interactions. Helices 6 and 8 pack side by side; tertiary RNA interactions, which also involve the strictly conserved tetraloop bases, stabilize helix 8 in a conformation competent for SRP54 binding. The structure explains the role of SRP19 and provides a molecular framework for SRP54 binding and SRP assembly in Eukarya and Archaea. |
==About this Structure== | ==About this Structure== | ||
| - | 1LNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNG 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: MG]] | [[Category: MG]] | ||
[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:32 2008'' |
Revision as of 11:46, 21 February 2008
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Crystal Structure of the SRP19-7S.S SRP RNA Complex of M. jannaschii
Overview
The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein. It associates with ribosomes to mediate co-translational targeting of membrane and secretory proteins to biological membranes. In mammalian cells, the SRP consists of a 7S RNA and six protein components. The S domain of SRP comprises the 7S.S part of RNA bound to SRP19, SRP54 and the SRP68/72 heterodimer; SRP54 has the main role in recognizing signal sequences of nascent polypeptide chains and docking SRP to its receptor. During assembly of the SRP, binding of SRP19 precedes and promotes the association of SRP54 (refs 4, 5). Here we report the crystal structure at 2.3 A resolution of the complex formed between 7S.S RNA and SRP19 in the archaeon Methanococcus jannaschii. SRP19 bridges the tips of helices 6 and 8 of 7S.S RNA by forming an extensive network of direct protein RNA interactions. Helices 6 and 8 pack side by side; tertiary RNA interactions, which also involve the strictly conserved tetraloop bases, stabilize helix 8 in a conformation competent for SRP54 binding. The structure explains the role of SRP19 and provides a molecular framework for SRP54 binding and SRP assembly in Eukarya and Archaea.
About this Structure
1LNG is a Single protein structure of sequence from Methanocaldococcus jannaschii with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the SRP19 RNA complex and implications for signal recognition particle assembly., Hainzl T, Huang S, Sauer-Eriksson AE, Nature. 2002 Jun 13;417(6890):767-71. Epub 2002 Jun 5. PMID:12050674
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