4uyk: Difference between revisions
New page: '''Unreleased structure''' The entry 4uyk is ON HOLD Authors: Bousset, L., Mary, C., Brooks, M.A., Scherrer, A., Strub, K., Cusack, S. Description: Crystal structure of a Signal Recogn... |
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The | ==Crystal structure of a Signal Recognition Particle Alu domain in the elongation arrest conformation== | ||
<StructureSection load='4uyk' size='340' side='right'caption='[[4uyk]], [[Resolution|resolution]] 3.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uyk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UYK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.22Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uyk OCA], [https://pdbe.org/4uyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uyk RCSB], [https://www.ebi.ac.uk/pdbsum/4uyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uyk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SRP09_HUMAN SRP09_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The signal recognition particle (SRP) is a conserved ribonucleoprotein particle that targets membrane and secreted proteins to translocation channels in membranes. In eukaryotes, the Alu domain, which comprises the 5' and 3' extremities of the SRP RNA bound to the SRP9/14 heterodimer, is thought to interact with the ribosome to pause translation elongation during membrane docking. We present the 3.2 A resolution crystal structure of a chimeric Alu domain, comprising Alu RNA from the archaeon Pyrococcus horikoshii bound to the human Alu binding proteins SRP9/14. The structure reveals how intricate tertiary interactions stabilize the RNA 5' domain structure and how an extra, archaeal-specific, terminal stem helps constrain the Alu RNA into the active closed conformation. In this conformation, highly conserved noncanonical base pairs allow unusually tight side-by-side packing of 5' and 3' RNA stems within the SRP9/14 RNA binding surface. The biological relevance of this structure is confirmed by showing that a reconstituted full-length chimeric archaeal-human SRP is competent to elicit elongation arrest in vitro. The structure will be useful in refining our understanding of how the SRP Alu domain interacts with the ribosome. | |||
Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation.,Bousset L, Mary C, Brooks MA, Scherrer A, Strub K, Cusack S RNA. 2014 Oct 21. PMID:25336584<ref>PMID:25336584</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uyk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Bousset L]] | |||
[[Category: Brooks MA]] | |||
[[Category: Cusack S]] | |||
[[Category: Mary C]] | |||
[[Category: Scherrer A]] | |||
[[Category: Strub K]] | |||
Latest revision as of 09:53, 17 October 2024
Crystal structure of a Signal Recognition Particle Alu domain in the elongation arrest conformationCrystal structure of a Signal Recognition Particle Alu domain in the elongation arrest conformation
Structural highlights
FunctionSRP09_HUMAN Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. Publication Abstract from PubMedThe signal recognition particle (SRP) is a conserved ribonucleoprotein particle that targets membrane and secreted proteins to translocation channels in membranes. In eukaryotes, the Alu domain, which comprises the 5' and 3' extremities of the SRP RNA bound to the SRP9/14 heterodimer, is thought to interact with the ribosome to pause translation elongation during membrane docking. We present the 3.2 A resolution crystal structure of a chimeric Alu domain, comprising Alu RNA from the archaeon Pyrococcus horikoshii bound to the human Alu binding proteins SRP9/14. The structure reveals how intricate tertiary interactions stabilize the RNA 5' domain structure and how an extra, archaeal-specific, terminal stem helps constrain the Alu RNA into the active closed conformation. In this conformation, highly conserved noncanonical base pairs allow unusually tight side-by-side packing of 5' and 3' RNA stems within the SRP9/14 RNA binding surface. The biological relevance of this structure is confirmed by showing that a reconstituted full-length chimeric archaeal-human SRP is competent to elicit elongation arrest in vitro. The structure will be useful in refining our understanding of how the SRP Alu domain interacts with the ribosome. Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation.,Bousset L, Mary C, Brooks MA, Scherrer A, Strub K, Cusack S RNA. 2014 Oct 21. PMID:25336584[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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