1mfq: Difference between revisions

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[[Image:1mfq.gif|left|200px]]<br />

[[Image:1mfq.gif|left|200px]]<br /><applet load="1mfq" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1mfq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1mfq, resolution 3.10Å" />

'''Crystal Structure Analysis of a Ternary S-Domain Complex of Human Signal Recognition Particle'''<br />

==Overview==

The eukaryotic signal recognition particle (SRP) is a cytoplasmic, ribonucleoprotein particle that targets secretory and membrane proteins to, the endoplasmic reticulum. The binding of SRP54 to the S domain of 7SL RNA, is highly dependent on SRP19. Here we present the crystal structure of a, human SRP ternary complex consisting of SRP19, the M domain of SRP54 and, the S domain of 7SL RNA. Upon binding of the M domain of SRP54 to the 7SL, RNA-SRP19 complex, the asymmetric loop of helix 8 in 7SL RNA collapses., The bases of the four nucleotides in the long strand of the asymmetric, loop continuously stack and interact with the M domain, whereas the two, adenines in the short strand flip out and form two A-minor motifs with, helix 6. This stabilizing interaction is only possible when helix 6 has, been positioned parallel to helix 8 by the prior binding of SRP19 to the, tetraloops of helices 6 and 8. Hence, the crystal structure of the ternary, complex suggests why SRP19 is necessary for the stable binding of SRP54 to, the S domain RNA.

The eukaryotic signal recognition particle (SRP) is a cytoplasmic ribonucleoprotein particle that targets secretory and membrane proteins to the endoplasmic reticulum. The binding of SRP54 to the S domain of 7SL RNA is highly dependent on SRP19. Here we present the crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA. Upon binding of the M domain of SRP54 to the 7SL RNA-SRP19 complex, the asymmetric loop of helix 8 in 7SL RNA collapses. The bases of the four nucleotides in the long strand of the asymmetric loop continuously stack and interact with the M domain, whereas the two adenines in the short strand flip out and form two A-minor motifs with helix 6. This stabilizing interaction is only possible when helix 6 has been positioned parallel to helix 8 by the prior binding of SRP19 to the tetraloops of helices 6 and 8. Hence, the crystal structure of the ternary complex suggests why SRP19 is necessary for the stable binding of SRP54 to the S domain RNA.

==About this Structure==

1MFQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MFQ OCA].

1MFQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFQ OCA].

==Reference==

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[[Category: rna-protein complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:10:47 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1mfq.gif|left|200px]]<br />
+[[Image:1mfq.gif|left|200px]]<br /><applet load="1mfq" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1mfq" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1mfq, resolution 3.10&Aring;" />
 '''Crystal Structure Analysis of a Ternary S-Domain Complex of Human Signal Recognition Particle'''<br />
 ==Overview==
-The eukaryotic signal recognition particle (SRP) is a cytoplasmic, ribonucleoprotein particle that targets secretory and membrane proteins to, the endoplasmic reticulum. The binding of SRP54 to the S domain of 7SL RNA, is highly dependent on SRP19. Here we present the crystal structure of a, human SRP ternary complex consisting of SRP19, the M domain of SRP54 and, the S domain of 7SL RNA. Upon binding of the M domain of SRP54 to the 7SL, RNA-SRP19 complex, the asymmetric loop of helix 8 in 7SL RNA collapses., The bases of the four nucleotides in the long strand of the asymmetric, loop continuously stack and interact with the M domain, whereas the two, adenines in the short strand flip out and form two A-minor motifs with, helix 6. This stabilizing interaction is only possible when helix 6 has, been positioned parallel to helix 8 by the prior binding of SRP19 to the, tetraloops of helices 6 and 8. Hence, the crystal structure of the ternary, complex suggests why SRP19 is necessary for the stable binding of SRP54 to, the S domain RNA.
+The eukaryotic signal recognition particle (SRP) is a cytoplasmic ribonucleoprotein particle that targets secretory and membrane proteins to the endoplasmic reticulum. The binding of SRP54 to the S domain of 7SL RNA is highly dependent on SRP19. Here we present the crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA. Upon binding of the M domain of SRP54 to the 7SL RNA-SRP19 complex, the asymmetric loop of helix 8 in 7SL RNA collapses. The bases of the four nucleotides in the long strand of the asymmetric loop continuously stack and interact with the M domain, whereas the two adenines in the short strand flip out and form two A-minor motifs with helix 6. This stabilizing interaction is only possible when helix 6 has been positioned parallel to helix 8 by the prior binding of SRP19 to the tetraloops of helices 6 and 8. Hence, the crystal structure of the ternary complex suggests why SRP19 is necessary for the stable binding of SRP54 to the S domain RNA.
 ==About this Structure==
-MFQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MFQ OCA].
+MFQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFQ OCA].
 ==Reference==
@@ Line 23: / Line 22: @@
 [[Category: rna-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:10:47 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:47 2008''