2ldo: Difference between revisions
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< | ==Solution structure of triheme cytochrome PpcA from Geobacter sulfurreducens reveals the structural origin of the redox-Bohr effect== | ||
<StructureSection load='2ldo' size='340' side='right'caption='[[2ldo]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ldo]] 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=2LDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2ldo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldo OCA], [https://pdbe.org/2ldo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldo RCSB], [https://www.ebi.ac.uk/pdbsum/2ldo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8GGK7_GEOSN Q8GGK7_GEOSN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Geobacter sulfurreducens (Gs) can transfer electrons to the exterior of its cells, a property that makes it a preferential candidate for the development of biotechnological applications. Its genome encodes for over one hundred cytochromes and despite their abundance and key functional roles, to date there is no structural information for these proteins in solution. The trihaem cytochrome PpcA has a crucial role in the conversion of electronic energy into proton motive force, a fundamental step for ATP synthesis in the presence of extracellular electron acceptors. In this work, 15N-labelled PpcA was produced and NMR spectroscopy was used to determine its solution structure in the fully reduced state, its backbone dynamics and the pH-dependent conformational changes. The structure obtained is well defined, with an average pairwise root-mean-square deviation of 0.25 A for the backbone atoms and 0.99 A for all heavy atoms, and constitutes the first solution structure of a Gs cytochrome. The redox-Bohr centre responsible for controlling the electron/proton transfer was identified, as well as the putative interacting regions between PpcA and its redox partners. The solution structure of PpcA will constitute the foundation for studies aimed at mapping out in detail these interacting regions. | |||
Revealing the structural origin of the redox-Bohr effect: the first solution structure of a cytochrome from Geobacter sulfurreducens.,Morgado L, Paixao VB, Schiffer M, Pokkuluri PR, Bruix M, Salgueiro CA Biochem J. 2011 Aug 24. PMID:21861844<ref>PMID:21861844</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ldo" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[Cytochrome | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Geobacter sulfurreducens]] | [[Category: Geobacter sulfurreducens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bruix M]] | ||
[[Category: | [[Category: Morgado L]] | ||
[[Category: | [[Category: Paixao VB]] | ||
[[Category: | [[Category: Salgueiro CA]] | ||
Latest revision as of 04:09, 21 November 2024
Solution structure of triheme cytochrome PpcA from Geobacter sulfurreducens reveals the structural origin of the redox-Bohr effectSolution structure of triheme cytochrome PpcA from Geobacter sulfurreducens reveals the structural origin of the redox-Bohr effect
Structural highlights
FunctionPublication Abstract from PubMedGeobacter sulfurreducens (Gs) can transfer electrons to the exterior of its cells, a property that makes it a preferential candidate for the development of biotechnological applications. Its genome encodes for over one hundred cytochromes and despite their abundance and key functional roles, to date there is no structural information for these proteins in solution. The trihaem cytochrome PpcA has a crucial role in the conversion of electronic energy into proton motive force, a fundamental step for ATP synthesis in the presence of extracellular electron acceptors. In this work, 15N-labelled PpcA was produced and NMR spectroscopy was used to determine its solution structure in the fully reduced state, its backbone dynamics and the pH-dependent conformational changes. The structure obtained is well defined, with an average pairwise root-mean-square deviation of 0.25 A for the backbone atoms and 0.99 A for all heavy atoms, and constitutes the first solution structure of a Gs cytochrome. The redox-Bohr centre responsible for controlling the electron/proton transfer was identified, as well as the putative interacting regions between PpcA and its redox partners. The solution structure of PpcA will constitute the foundation for studies aimed at mapping out in detail these interacting regions. Revealing the structural origin of the redox-Bohr effect: the first solution structure of a cytochrome from Geobacter sulfurreducens.,Morgado L, Paixao VB, Schiffer M, Pokkuluri PR, Bruix M, Salgueiro CA Biochem J. 2011 Aug 24. PMID:21861844[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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