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[[Image:1ffh.gif|left|200px]]<br /><applet load="1ffh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ffh, resolution 2.05&Aring;" />
'''N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS'''<br />


==Overview==
==N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS==
The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein-ribosome complexes to the membrane translocation apparatus. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-alpha subunit (termed FtsY). Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides. Sequence conservation suggests that structurally similar N and G domains are present in FtsY. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily.
<StructureSection load='1ffh' size='340' side='right'caption='[[1ffh]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ffh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFH 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]] 2.05&#8491;</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></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=1ffh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffh OCA], [https://pdbe.org/1ffh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffh RCSB], [https://www.ebi.ac.uk/pdbsum/1ffh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]
== 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/ff/1ffh_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=1ffh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=I:Gtpase+Binding+Site+Identified+By+Conserved+Motifs+I-Iv'>I</scene>, <scene name='pdbsite=II:Gtpase+Binding+Site+Identified+By+Conserved+Motifs+I-Iv'>II</scene>, <scene name='pdbsite=III:Gtpase+Binding+Site+Identified+By+Conserved+Motifs+I-Iv'>III</scene> and <scene name='pdbsite=IV:Gtpase+Binding+Site+Identified+By+Conserved+Motifs+I-Iv'>IV</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFH OCA].
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of the conserved GTPase domain of the signal recognition particle., Freymann DM, Keenan RJ, Stroud RM, Walter P, Nature. 1997 Jan 23;385(6614):361-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9002524 9002524]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Freymann, D M.]]
[[Category: Freymann DM]]
[[Category: Keenan, R J.]]
[[Category: Keenan RJ]]
[[Category: Stroud, R M.]]
[[Category: Stroud RM]]
[[Category: Walter, P.]]
[[Category: Walter P]]
[[Category: MG]]
[[Category: ffh]]
[[Category: gtpase]]
[[Category: ribonucleoprotein]]
[[Category: signal recognition particle]]
[[Category: srp]]
 
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Retrieved from "https://proteopedia.org/1ffh"