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==Solution structure of oxidized triheme cytochrome PpcA from Geobacter sulfurreducens==
==Solution structure of oxidized triheme cytochrome PpcA from Geobacter sulfurreducens==
<StructureSection load='2mz9' size='340' side='right'caption='[[2mz9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2mz9' size='340' side='right'caption='[[2mz9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mz9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51573 Atcc 51573]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZ9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mz9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacter_sulfurreducens Geobacter sulfurreducens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZ9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppcA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35554 ATCC 51573])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=2mz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mz9 OCA], [https://pdbe.org/2mz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mz9 RCSB], [https://www.ebi.ac.uk/pdbsum/2mz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mz9 ProSAT]</span></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=2mz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mz9 OCA], [https://pdbe.org/2mz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mz9 RCSB], [https://www.ebi.ac.uk/pdbsum/2mz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mz9 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8GGK7_GEOSN Q8GGK7_GEOSN]
The periplasmic triheme cytochrome PpcA from Geobacter sulfurreducens is highly abundant; it is the likely reservoir of electrons to the outer surface to assist the reduction of extracellular terminal acceptors; these include insoluble metal oxides in natural habitats and electrode surfaces from which electricity can be harvested. A detailed thermodynamic characterization of PpcA showed that it has an important redox-Bohr effect that might implicate the protein in e-/H+ coupling mechanisms to sustain cellular growth. This functional mechanism requires control of both the redox state and the protonation state. In the present study, isotope-labeled PpcA was produced and the three-dimensional structure of PpcA in the oxidized form was determined by NMR. This is the first solution structure of a G. sulfurreducens cytochrome in the oxidized state. The comparison of oxidized and reduced structures revealed that the heme I axial ligand geometry changed and there were other significant changes in the segments near heme I. The pH-linked conformational rearrangements observed in the vicinity of the redox-Bohr center, both in the oxidized and reduced structures, constitute the structural basis for the differences observed in the pKa values of the redox-Bohr center, providing insights into the e-/H+ coupling molecular mechanisms driven by PpcA in G. sulfurreducens.
 
Redox- and pH-linked conformational changes in triheme cytochrome PpcA from Geobacter sulfurreducens.,Morgado L, Bruix M, Pokkuluri PR, Salgueiro CA, Turner DL Biochem J. 2017 Jan 15;474(2):231-246. doi: 10.1042/BCJ20160932. Epub 2016 Nov, 14. PMID:28062839<ref>PMID:28062839</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mz9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 51573]]
[[Category: Geobacter sulfurreducens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bruix, M]]
[[Category: Bruix M]]
[[Category: Morgado, L]]
[[Category: Morgado L]]
[[Category: Pokkuluri, R]]
[[Category: Pokkuluri R]]
[[Category: Salgueiro, C A]]
[[Category: Salgueiro CA]]
[[Category: Turner, D L]]
[[Category: Turner DL]]
[[Category: Cytochrome]]
[[Category: Electron transport]]
[[Category: Paramagnetic]]

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