6h5l
From Proteopedia
(Difference between revisions)
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<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'>[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> | ||
</table> | </table> | ||
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:50, 17 April 2019
Kuenenia stuttgartiensis reducing HAO-like protein complex Kustc0457/Kustc0458
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