3e70: Difference between revisions
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==Structures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus Furiosus== | |||
<StructureSection load='3e70' size='340' side='right'caption='[[3e70]], [[Resolution|resolution]] 1.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3e70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E70 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]] 1.97Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3e70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e70 OCA], [https://pdbe.org/3e70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e70 RCSB], [https://www.ebi.ac.uk/pdbsum/3e70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e70 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8U051_PYRFU Q8U051_PYRFU] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity).[HAMAP-Rule:MF_00920] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In all organisms, a ribonucleoprotein called the signal recognition particle (SRP) and its receptor (SR) target nascent proteins from the ribosome to the translocon for secretion or membrane insertion. We present the first X-ray structures of an archeal FtsY, the receptor from the hyper-thermophile Pyrococcus furiosus (Pfu), in its free and GDP*magnesium-bound forms. The highly charged N-terminal domain of Pfu-FtsY is distinguished by a long N-terminal helix. The basic charges on the surface of this helix are likely to regulate interactions at the membrane. A peripheral GDP bound near a regulatory motif could indicate a site of interaction between the receptor and ribosomal or SRP RNAs. Small angle X-ray scattering and analytical ultracentrifugation indicate that the crystal structure of Pfu-FtsY correlates well with the average conformation in solution. Based on previous structures of two sub-complexes, we propose a model of the core of archeal and eukaryotic SRP*SR targeting complexes. | |||
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.,Egea PF, Tsuruta H, de Leon GP, Napetschnig J, Walter P, Stroud RM PLoS ONE. 2008;3(11):e3619. Epub 2008 Nov 3. PMID:18978942<ref>PMID:18978942</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3e70" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Signal recognition particle receptor|Signal recognition particle receptor]] | *[[Signal recognition particle receptor|Signal recognition particle receptor]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Egea | [[Category: Egea PF]] | ||
[[Category: Napetschnig | [[Category: Napetschnig J]] | ||
[[Category: Stroud | [[Category: Stroud RM]] | ||
[[Category: Tsuruta | [[Category: Tsuruta H]] | ||
[[Category: Walter | [[Category: Walter P]] | ||
Latest revision as of 15:59, 30 August 2023
Structures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus FuriosusStructures and conformations in solution of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus Furiosus
Structural highlights
FunctionQ8U051_PYRFU Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (By similarity).[HAMAP-Rule:MF_00920] Publication Abstract from PubMedIn all organisms, a ribonucleoprotein called the signal recognition particle (SRP) and its receptor (SR) target nascent proteins from the ribosome to the translocon for secretion or membrane insertion. We present the first X-ray structures of an archeal FtsY, the receptor from the hyper-thermophile Pyrococcus furiosus (Pfu), in its free and GDP*magnesium-bound forms. The highly charged N-terminal domain of Pfu-FtsY is distinguished by a long N-terminal helix. The basic charges on the surface of this helix are likely to regulate interactions at the membrane. A peripheral GDP bound near a regulatory motif could indicate a site of interaction between the receptor and ribosomal or SRP RNAs. Small angle X-ray scattering and analytical ultracentrifugation indicate that the crystal structure of Pfu-FtsY correlates well with the average conformation in solution. Based on previous structures of two sub-complexes, we propose a model of the core of archeal and eukaryotic SRP*SR targeting complexes. Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.,Egea PF, Tsuruta H, de Leon GP, Napetschnig J, Walter P, Stroud RM PLoS ONE. 2008;3(11):e3619. Epub 2008 Nov 3. PMID:18978942[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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