View source for 7a58


==NOE-only solution structure of the Iron-Sulfur protein PioC from Rhodopseudomonas palustris TIE-1==
<StructureSection load='7a58' size='340' side='right'caption='[[7a58]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7a58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhopt Rhopt]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A58 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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;'>[[6xyv|6xyv]], [[7a4l|7a4l]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rpal_0815 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=395960 RHOPT])</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=7a58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a58 OCA], [https://pdbe.org/7a58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a58 RCSB], [https://www.ebi.ac.uk/pdbsum/7a58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a58 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Metalloproteins play key roles across biology, and knowledge of their structure is essential to understand their physiological role. For those metalloproteins containing paramagnetic states, the enhanced relaxation caused by the unpaired electrons often makes signal detection unfeasible near the metal center, precluding adequate structural characterization right where it is more biochemically relevant. Here, we report a protein structure determination by NMR where two different sets of restraints, one containing Nuclear Overhauser Enhancements (NOEs) and another containing Paramagnetic Relaxation Enhancements (PREs), are used separately and eventually together. The protein PioC from Rhodopseudomonas palustris TIE-1 is a High Potential Iron-Sulfur Protein (HiPIP) where the [4Fe-4S] cluster is paramagnetic in both oxidation states at room temperature providing the source of PREs used as alternative distance restraints. Comparison of the family of structures obtained using NOEs only, PREs only and the combination of both reveals that the pairwise root-mean-square deviation (RMSD) between them are similar and comparable with the precision within each family. This demonstrates that, under favorable conditions in terms of protein size and paramagnetic effects, PREs can efficiently complement and eventually replace NOEs for the structural characterization of small paramagnetic metalloproteins and denovo designed metalloproteins by NMR.

PRE-driven Protein NMR Structures: an Alternative Approach in Highly Paramagnetic Systems.,Trindade IB, Invernici M, Cantini F, Louro RO, Piccioli M FEBS J. 2020 Oct 30. doi: 10.1111/febs.15615. PMID:33124176<ref>PMID:33124176</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7a58" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhopt]]
[[Category: Cantini, F]]
[[Category: Trindade, I]]
[[Category: Electron transport]]
[[Category: Iron-sulphur protein]]
[[Category: Metallo protein]]
[[Category: Paramagnetic nmr]]
[[Category: Paramagnetic protein]]
[[Category: Solution structure by nmr]]