6H5L
Kuenenia stuttgartiensis reducing HAO-like protein complex Kustc0457/Kustc0458
Summary for 6H5L
| Entry DOI | 10.2210/pdb6h5l/pdb |
| Descriptor | Similar to hydroxylamine oxidoreductase, Conserved hypothetical cytochrome protein, HEME C, ... (4 entities in total) |
| Functional Keywords | reductase, anammox, oxidoreductase |
| Biological source | Kuenenia stuttgartiensis More |
| Total number of polymer chains | 2 |
| Total formula weight | 91442.00 |
| Authors | Dietl, A.,Maalcke, W.,Barends, T.R.M. (deposition date: 2018-07-25, release date: 2019-04-10, Last modification date: 2024-10-23) |
| Primary citation | Dietl, A.,Maalcke, W.J.,Ferousi, C.,Jetten, M.S.M.,Kartal, B.,Barends, T.R.M. A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway. Acta Crystallogr D Struct Biol, 75:333-341, 2019 Cited by PubMed Abstract: 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 Å resolution shows a heterododecameric (αβ) 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. PubMed: 30950404DOI: 10.1107/S2059798318017473 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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