View source for 3lx5


==Crystal structure of mGMPPNP-bound NFeoB from S. thermophilus==
<StructureSection load='3lx5' size='340' side='right'caption='[[3lx5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lx5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus_LMG_18311 Streptococcus thermophilus LMG 18311]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LX5 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGO:2-AMINO-9-(5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}PHOSPHORYL]-3-O-{[2-(METHYLAMINO)PHENYL]CARBONYL}-BETA-D-ERYTHRO-PENTOFURANOSYL-2-ULOSE)-1,9-DIHYDRO-6H-PURIN-6-ONE'>AGO</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'>[https://proteopedia.org/fgij/fg.htm?mol=3lx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lx5 OCA], [https://pdbe.org/3lx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3lx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lx5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5M586_STRT2 Q5M586_STRT2] 
== 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/lx/3lx5_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=3lx5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
FeoB is a prokaryotic membrane protein responsible for the import of ferrous iron (Fe(2+)). A defining feature of FeoB is that it includes an N-terminal 30-kDa soluble domain with GTPase activity, which is required for iron transport. However, the low intrinsic GTP hydrolysis rate of this domain appears to be too slow for FeoB either to function as a channel or to possess an active Fe(2+) membrane transport mechanism. Here, we present crystal structures of the soluble domain of FeoB from Streptococcus thermophilus in complex with GDP and with the GTP analogue derivative 2'-(or -3')-O-(N-methylanthraniloyl)-beta,gamma-imidoguanosine 5'-triphosphate (mant-GMPPNP). Unlike recent structures of the G protein domain, the mant-GMPPNP-bound structure shows clearly resolved, active conformations of the critical Switch motifs. Importantly, biochemical analyses demonstrate that the GTPase activity of FeoB is activated by K(+), which leads to a 20-fold acceleration in its hydrolysis rate. Analysis of the structure identified a conserved asparagine residue likely to be involved in K(+) coordination, and mutation of this residue abolished K(+)-dependent activation. We suggest that this, together with a second asparagine residue that we show is critical for the structure of the Switch I loop, allows the prediction of K(+)-dependent activation in G proteins. In addition, the accelerated hydrolysis rate opens up the possibility that FeoB might indeed function as an active transporter.

Potassium-activated GTPase reaction in the G Protein-coupled ferrous iron transporter B.,Ash MR, Guilfoyle A, Clarke RJ, Guss JM, Maher MJ, Jormakka M J Biol Chem. 2010 May 7;285(19):14594-602. Epub 2010 Mar 10. PMID:20220129<ref>PMID:20220129</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 3lx5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus thermophilus LMG 18311]]
[[Category: Ash MR]]
[[Category: Clarke RJ]]
[[Category: Guilfoyle A]]
[[Category: Guss JM]]
[[Category: Jormakka M]]
[[Category: Maher MJ]]