Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes
© Daisuke Sasaki et al. 2020..
Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitro-gen cycle where nitrate is used in place of di-oxy-gen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the Hyphomicrobium denitrificans strain 1NES1 (Hd 1NES1NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2020 |
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Erschienen: |
2020 |
Enthalten in: |
Zur Gesamtaufnahme - volume:7 |
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Enthalten in: |
IUCrJ - 7(2020), Pt 3 vom: 01. Mai, Seite 557-565 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Sasaki, Daisuke [VerfasserIn] |
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Links: |
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Themen: |
Catalysis |
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Anmerkungen: |
Date Revised 13.11.2023 published: Electronic-eCollection Citation Status PubMed-not-MEDLINE |
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doi: |
10.1107/S2052252520005230 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM310142571 |
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245 | 1 | 0 | |a Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
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520 | |a © Daisuke Sasaki et al. 2020. | ||
520 | |a Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitro-gen cycle where nitrate is used in place of di-oxy-gen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the Hyphomicrobium denitrificans strain 1NES1 (Hd 1NES1NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a catalysis | |
650 | 4 | |a copper-containing nitrite reductase | |
650 | 4 | |a denitrification | |
650 | 4 | |a electron transfer | |
650 | 4 | |a nitrogen cycle | |
650 | 4 | |a structural biology | |
700 | 1 | |a Watanabe, Tatiana F |e verfasserin |4 aut | |
700 | 1 | |a Eady, Robert R |e verfasserin |4 aut | |
700 | 1 | |a Garratt, Richard C |e verfasserin |4 aut | |
700 | 1 | |a Antonyuk, Svetlana V |e verfasserin |4 aut | |
700 | 1 | |a Hasnain, S Samar |e verfasserin |4 aut | |
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