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New page: left|200px<br /><applet load="1ls1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ls1, resolution 1.10Å" /> '''T. aquaticus Ffh NG ...
 
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[[Image:1ls1.gif|left|200px]]<br /><applet load="1ls1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ls1, resolution 1.10&Aring;" />
'''T. aquaticus Ffh NG Domain at 1.1A Resolution'''<br />


==Overview==
==T. aquaticus Ffh NG Domain at 1.1A Resolution==
The NG domain of the prokaryotic signal recognition protein Ffh is a, two-domain GTPase that comprises part of the prokaryotic signal, recognition particle (SRP) that functions in co-translational targeting of, proteins to the membrane. The interface between the N and G domains, includes two highly conserved sequence motifs and is adjacent in sequence, and structure to one of the conserved GTPase signature motifs. Previous, structural studies have shown that the relative orientation of the two, domains is dynamic. The N domain of Ffh has been proposed to function in, regulating the nucleotide-binding interactions of the G domain. However, biochemical studies suggest a more complex role for the domain in, integrating communication between signal sequence recognition and, interaction with receptor. Here, we report the structure of the apo NG, GTPase of Ffh from Thermus aquaticus refined at 1.10 A resolution., Although the G domain is very well ordered in this structure, the N domain, is less well ordered, reflecting the dynamic relationship between the two, domains previously inferred. We demonstrate that the anisotropic, displacement parameters directly visualize the underlying mobility between, the two domains, and present a detailed structural analysis of the packing, of the residues, including the critical alpha4 helix, that comprise the, interface. Our data allows us to propose a structural explanation for the, functional significance of sequence elements conserved at the N/G, interface.
<StructureSection load='1ls1' size='340' side='right'caption='[[1ls1]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ls1]] 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=1LS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LS1 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]] 1.1&#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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1ls1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ls1 OCA], [https://pdbe.org/1ls1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ls1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ls1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ls1 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/ls/1ls1_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=1ls1 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LS1 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 MG and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LS1 OCA].
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh., Ramirez UD, Minasov G, Focia PJ, Stroud RM, Walter P, Kuhn P, Freymann DM, J Mol Biol. 2002 Jul 19;320(4):783-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12095255 12095255]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Freymann, D.M.]]
[[Category: Freymann DM]]
[[Category: Minasov, G.]]
[[Category: Minasov G]]
[[Category: Ramirez, U.D.]]
[[Category: Ramirez UD]]
[[Category: MG]]
[[Category: OXY]]
[[Category: ffh]]
[[Category: gtpase]]
[[Category: srp]]
[[Category: srp54]]
[[Category: ultrahigh resolution]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:49:35 2007''

Latest revision as of 07:35, 14 February 2024

T. aquaticus Ffh NG Domain at 1.1A Resolution

1ls1, resolution 1.10Å

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