Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase.
Analytical ultracentrifugation
Assimilatory NADPH-dependent sulfite reductase
Electron transfer
Oxidoreductase
Solution scattering
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
received:
06
01
2021
revised:
04
03
2021
accepted:
08
03
2021
pubmed:
17
3
2021
medline:
27
1
2022
entrez:
16
3
2021
Statut:
ppublish
Résumé
Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur for biomass incorporation. Electron transfer within SiR requires intra- and inter-subunit interactions that are mediated by the relative position of each protein, governed by flexible domain movements. Using small-angle neutron scattering, we report the first solution structures of SiR heterodimers containing a single copy of each subunit. These structures show how the subunits bind and how both subunit binding and oxidation state impact SiRFP's conformation. Neutron contrast matching experiments on selectively deuterated heterodimers allow us to define the contribution of each subunit to the solution scattering. SiRHP binding induces a change in the position of SiRFP's flavodoxin-like domain relative to its ferredoxin-NADP
Identifiants
pubmed: 33722582
pii: S1047-8477(21)00029-0
doi: 10.1016/j.jsb.2021.107724
pii:
doi:
Substances chimiques
Ferredoxins
0
Protein Subunits
0
Solutions
0
Solvents
0
Sulfite Reductase (NADPH)
EC 1.8.1.2
sulfite reductase (NADPH), E coli
EC 1.8.1.2
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
107724Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.