View source for 2og2


==Crystal structure of chloroplast FtsY from Arabidopsis thaliana==
<StructureSection load='2og2' size='340' side='right'caption='[[2og2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2og2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OG2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zu4|1zu4]], [[1zu5|1zu5]], [[1rj9|1rj9]], [[1vma|1vma]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsY ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=2og2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2og2 OCA], [https://pdbe.org/2og2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2og2 RCSB], [https://www.ebi.ac.uk/pdbsum/2og2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2og2 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://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>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/2og2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2og2 ConSurf].
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== Publication Abstract from PubMed ==
The signal recognition particle (SRP) pathway mediates co-translational targeting of nascent proteins to membranes. Chloroplast SRP is unique in that it does not contain the otherwise universally conserved SRP RNA, which accelerates the association between the SRP guanosine-5'-triphosphate (GTP) binding protein and its receptor FtsY in classical SRP pathways. Recently, we showed that the SRP and SRP receptor (SR) GTPases from chloroplast (cpSRP54 and cpFtsY, respectively) can interact with one another 400-fold more efficiently than their bacterial homologues, thus providing an explanation as to why this novel chloroplast SRP pathway bypasses the requirement for the SRP RNA. Here we report the crystal structure of cpFtsY from Arabidopsis thaliana at 2.0 A resolution. In this chloroplast SR, the N-terminal "N" domain is more tightly packed, and a more extensive interaction surface is formed between the GTPase "G" domain and the N domain than was previously observed in many of its bacterial homologues. As a result, the overall conformation of apo-cpFtsY is closer to that found in the bacterial SRP*FtsY complex than in free bacterial FtsY, especially with regard to the relative orientation of the N and G domains. In contrast, active-site residues in the G domain are mispositioned, explaining the low basal GTP binding and hydrolysis activity of free cpFtsY. This structure emphasizes proper N-G domain arrangement as a key factor in modulating the efficiency of SRP-receptor interaction and helps account, in part, for the faster kinetics at which the chloroplast SR interacts with its binding partner in the absence of an SRP RNA.

Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.,Chandrasekar S, Chartron J, Jaru-Ampornpan P, Shan SO J Mol Biol. 2008 Jan 11;375(2):425-36. Epub 2007 Nov 26. PMID:18035371<ref>PMID:18035371</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2og2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Large Structures]]
[[Category: Ampornpan, P J]]
[[Category: Chandrasekar, S]]
[[Category: Chartron, J]]
[[Category: Shan, S]]
[[Category: Nucleotide-binding]]
[[Category: Protein transport]]