3tah: Difference between revisions

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'''Unreleased structure'''


The entry 3tah is ON HOLD
==Crystal structure of an S. thermophilus NFeoB N11A mutant bound to mGDP==
<StructureSection load='3tah' size='340' side='right'caption='[[3tah]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tah]] is a 2 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=3TAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TAH 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGO:3-O-(N-METHYLANTHRANILOYL)GUANOSINE-5-DIPHOSPHATE'>BGO</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=3tah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tah OCA], [https://pdbe.org/3tah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tah RCSB], [https://www.ebi.ac.uk/pdbsum/3tah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tah ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5M586_STRT2 Q5M586_STRT2]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The uptake of ferrous iron in prokaryotes is mediated by the G-protein-coupled membrane protein FeoB. The protein contains two N-terminal soluble domains that are together called `NFeoB'. One of these is a G-protein domain, and GTP hydrolysis by this domain is essential for iron transport. The GTPase activity of NFeoB is accelerated in the presence of potassium ions, which bind at a site adjacent to the nucleotide. One of the ligands at the potassium-binding site is a conserved asparagine residue, which corresponds to Asn11 in Streptococcus thermophilus NFeoB. The structure of an N11A S. thermophilus NFeoB mutant has been determined and refined to a resolution of 1.85 A; the crystals contained a mixture of mant-GDP-bound and mant-GMP-bound protein. The structure demonstrates how the use of a derivatized nucleotide in cocrystallization experiments can facilitate the growth of diffraction-quality crystals.


Authors: Ash, M.R., Maher, M.J., Guss, J.M., Jormakka, M.
The structure of an N11A mutant of the G-protein domain of FeoB.,Ash MR, Maher MJ, Guss JM, Jormakka M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1511-5., Epub 2011 Nov 29. PMID:22139154<ref>PMID:22139154</ref>


Description: Crystal structure of an S. thermophilus NFeoB N11A mutant bound to mGDP
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tah" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus thermophilus LMG 18311]]
[[Category: Ash MR]]
[[Category: Guss JM]]
[[Category: Jormakka M]]
[[Category: Maher MJ]]
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