View source for 6h5l


==Kuenenia stuttgartiensis reducing HAO-like protein complex Kustc0457/Kustc0458==
<StructureSection load='6h5l' size='340' side='right'caption='[[6h5l]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=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>
== Function ==
[https://www.uniprot.org/uniprot/Q1PVE1_KUEST Q1PVE1_KUEST] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:30950404</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6h5l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candidatus Kuenenia stuttgartiensis]]
[[Category: Large Structures]]
[[Category: Barends TRM]]
[[Category: Dietl A]]
[[Category: Maalcke W]]