Structure determination of the HgcAB complex using metagenome sequence data: insights into microbial mercury methylation.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
19 06 2020
19 06 2020
Historique:
received:
27
01
2020
accepted:
27
05
2020
entrez:
21
6
2020
pubmed:
21
6
2020
medline:
24
6
2021
Statut:
epublish
Résumé
Bacteria and archaea possessing the hgcAB gene pair methylate inorganic mercury (Hg) to form highly toxic methylmercury. HgcA consists of a corrinoid binding domain and a transmembrane domain, and HgcB is a dicluster ferredoxin. However, their detailed structure and function have not been thoroughly characterized. We modeled the HgcAB complex by combining metagenome sequence data mining, coevolution analysis, and Rosetta structure calculations. In addition, we overexpressed HgcA and HgcB in Escherichia coli, confirmed spectroscopically that they bind cobalamin and [4Fe-4S] clusters, respectively, and incorporated these cofactors into the structural model. Surprisingly, the two domains of HgcA do not interact with each other, but HgcB forms extensive contacts with both domains. The model suggests that conserved cysteines in HgcB are involved in shuttling Hg
Identifiants
pubmed: 32561885
doi: 10.1038/s42003-020-1047-5
pii: 10.1038/s42003-020-1047-5
pmc: PMC7305189
doi:
Substances chimiques
Bacterial Proteins
0
Corrinoids
0
Multiprotein Complexes
0
Mercury
FXS1BY2PGL
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
320Subventions
Organisme : NIH HHS
ID : DP5 OD026389
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM124174
Pays : United States
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