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| | <StructureSection load='6h5l' size='340' side='right'caption='[[6h5l]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6h5l' size='340' side='right'caption='[[6h5l]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6h5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Kuenenia_stuttgartiensis Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H5L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6h5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Kuenenia_stuttgartiensis Candidatus Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H5L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxylamine_dehydrogenase Hydroxylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.6 1.7.2.6] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h5l OCA], [http://pdbe.org/6h5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h5l RCSB], [http://www.ebi.ac.uk/pdbsum/6h5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h5l 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=6h5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h5l OCA], [https://pdbe.org/6h5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h5l RCSB], [https://www.ebi.ac.uk/pdbsum/6h5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h5l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1PVE1_KUEST Q1PVE1_KUEST] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hydroxylamine dehydrogenase]] | + | [[Category: Candidatus Kuenenia stuttgartiensis]] |
| - | [[Category: Kuenenia stuttgartiensis]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barends, T R.M]] | + | [[Category: Barends TRM]] |
| - | [[Category: Dietl, A]] | + | [[Category: Dietl A]] |
| - | [[Category: Maalcke, W]] | + | [[Category: Maalcke W]] |
| - | [[Category: Anammox]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| Structural highlights
Function
Q1PVE1_KUEST
Publication Abstract from PubMed
The hydroxylamine oxidoreductase/hydrazine dehydrogenase (HAO/HDH) protein family constitutes an important group of octaheme cytochromes c (OCCs). The majority of these proteins form homotrimers, with their subunits being covalently attached to each other via a rare cross-link between the catalytic heme moiety and a conserved tyrosine residue in an adjacent subunit. This covalent cross-link has been proposed to modulate the active-site heme towards oxidative catalysis by distorting the heme plane. In this study, the crystal structure of a stable complex of an HAO homologue (KsHAOr) with its diheme cytochrome c redox partner (KsDH) from the anammox bacterium Kuenenia stuttgartiensis was determined. KsHAOr lacks the tyrosine cross-link and is therefore tuned to reductive catalysis. The molecular model of the KsHAOr-KsDH complex at 2.6 A resolution shows a heterododecameric (alpha6beta6) assembly, which was also shown to be the oligomeric state in solution by analytical ultracentrifugation and multi-angle static light scattering. The 60-heme-containing protein complex reveals a unique extended electron transfer pathway and provides deeper insights into catalysis and electron transfer in reductive OCCs.
A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway.,Dietl A, Maalcke WJ, Ferousi C, Jetten MSM, Kartal B, Barends TRM Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):333-341. doi:, 10.1107/S2059798318017473. Epub 2019 Feb 28. PMID:30950404[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dietl A, Maalcke WJ, Ferousi C, Jetten MSM, Kartal B, Barends TRM. A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway. Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):333-341. doi:, 10.1107/S2059798318017473. Epub 2019 Feb 28. PMID:30950404 doi:http://dx.doi.org/10.1107/S2059798318017473
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