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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
DOI:
10.1107/S2052252520005230
Authors:
Daisuke
Sasaki
(University of Liverpool)
,
Tatiana F.
Watanabe
(University of Liverpool; University of São Paulo)
,
Robert R.
Eady
(University of Liverpool)
,
Richard C.
Garratt
(University of São Paulo)
,
Svetlana V.
Antonyuk
(University of Liverpool)
,
S. Samar
Hasnain
(University of Liverpool)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Iucrj
, VOL 7
, PAGES 557 - 565
State:
Published (Approved)
Published:
May 2020
Diamond Proposal Number(s):
15991

Abstract: 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 nitrogen cycle where nitrate is used in place of dioxygen 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 (Hd1NES1NiR) 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.
Journal Keywords: nitrogen cycle; denitrification; copper-containing nitrite reductase; electron transfer; catalysis; structural biology
Diamond Keywords: Enzymes
Subject Areas:
Biology and Bio-materials
Instruments:
I04-Macromolecular Crystallography
Added On:
30/04/2020 13:44
Documents:
jt5044.pdf
Discipline Tags:
Biochemistry
Catalysis
Chemistry
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)