9rk3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Soluble domain of kustd1480, a Rieske iron-sulfur cluster protein from Kuenenia stuttgartiensis== | |
| + | <StructureSection load='9rk3' size='340' side='right'caption='[[9rk3]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9rk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Kuenenia_sp. Candidatus Kuenenia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RK3 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]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=9rk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rk3 OCA], [https://pdbe.org/9rk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rk3 RCSB], [https://www.ebi.ac.uk/pdbsum/9rk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rk3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q1PYR8_KUEST Q1PYR8_KUEST] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Anaerobic ammonium-oxidizing (anammox) bacteria employ a unique, hydrazine-based pathway to obtain energy from nitrite and ammonium. These organisms possess distinct Rieske/cytochrome b complexes whose precise role in anammox metabolism remains unclear, but which have been proposed to include the generation of NAD(P)H. This would require energetics and structural features unusual for such complexes. Here we present crystal structures and electrochemical investigations of the Rieske subunits of two of these complexes from the anammox organism Kuenenia stuttgartiensis, Kuste4569 and Kustd1480. Both proteins display high redox potentials (> + 300 mV), which can be in part explained by their crystal structures and which fit perfectly into the energetic scheme of the proposed NAD(P)H generation mechanism. Moreover, AlphaFold3 models of the parent complexes trace out a path for the electrons required for NAD(P)H production, which includes a proposed, novel b-type heme in the membrane-bound part of the complex. | ||
| - | + | Rieske Iron-Sulfur Cluster Proteins From an Anaerobic Ammonium Oxidizer Suggest Unusual Energetics in Their Parent Rieske/Cytochrome b Complexes.,Hauser D, Sode M, Andreeva EA, Parey K, Barends TRM Proteins. 2025 Nov 12. doi: 10.1002/prot.70084. PMID:41222066<ref>PMID:41222066</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9rk3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Barends | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Candidatus Kuenenia sp]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Barends T]] | ||
| + | [[Category: Hauser D]] | ||
Current revision
Soluble domain of kustd1480, a Rieske iron-sulfur cluster protein from Kuenenia stuttgartiensis
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