5l3r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
<table><tr><td colspan='2'>[[5l3r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L3R FirstGlance]. <br>
<table><tr><td colspan='2'>[[5l3r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L3R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3r OCA], [http://pdbe.org/5l3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l3r RCSB], [http://www.ebi.ac.uk/pdbsum/5l3r PDBsum]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3r OCA], [http://pdbe.org/5l3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l3r RCSB], [http://www.ebi.ac.uk/pdbsum/5l3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SR54C_ARATH SR54C_ARATH]] Involved in cotranslational and post-translational sorting of thylakoid proteins. Binds GTP specifically. Activates the GTPase activity of CPFTSY when bound together. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids.<ref>PMID:10480939</ref> <ref>PMID:11356852</ref> <ref>PMID:17475780</ref> <ref>PMID:18633119</ref> [[http://www.uniprot.org/uniprot/CFTSY_ARATH CFTSY_ARATH]] Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.<ref>PMID:10214972</ref> <ref>PMID:10480939</ref> <ref>PMID:12105232</ref> <ref>PMID:17475780</ref> <ref>PMID:18764927</ref> <ref>PMID:19293157</ref>
[[http://www.uniprot.org/uniprot/SR54C_ARATH SR54C_ARATH]] Involved in cotranslational and post-translational sorting of thylakoid proteins. Binds GTP specifically. Activates the GTPase activity of CPFTSY when bound together. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids.<ref>PMID:10480939</ref> <ref>PMID:11356852</ref> <ref>PMID:17475780</ref> <ref>PMID:18633119</ref> [[http://www.uniprot.org/uniprot/CFTSY_ARATH CFTSY_ARATH]] Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.<ref>PMID:10214972</ref> <ref>PMID:10480939</ref> <ref>PMID:12105232</ref> <ref>PMID:17475780</ref> <ref>PMID:18764927</ref> <ref>PMID:19293157</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life. Here, we present the crystal structures of the GTPase heterodimers of archaeal (Sulfolobus solfataricus), eukaryotic (Homo sapiens), and chloroplast (Arabidopsis thaliana) SRP systems. The comprehensive structural comparison combined with Brownian dynamics simulations of TC formation allows for the description of the general blueprint and of specific adaptations of the quasi-symmetric heterodimer. Our work defines conserved external nucleotide-binding sites for SRP GTPase activation by RNA. Structural analyses of the GDP-bound, post-hydrolysis states reveal a conserved, magnesium-sensitive switch within the I-box. Overall, we provide a general model for SRP cycle regulation by RNA.
 +
 +
Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex.,Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309<ref>PMID:27241309</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5l3r" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 06:54, 26 July 2016

Structure of the GTPase heterodimer of chloroplast SRP54 and FtsY from Arabidopsis thaliana

5l3r, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5l3r"
Personal tools