Diiron Enzyme Structure and Catalysis

Fox, Brian G.

doi:10.1016/b978-0-08-102688-5.00059-3

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2022

Publication Types

Select...

Article1

Book1

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 294 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ferritin‐like superfamily is composed by a large diversity of proteins sharing a common fold, constituted of an α‐helix bundle core housing a dinuclear metal centre [1,2]. Despite their similar architecture, members of this superfamily differ largely in sequence and perform a variety of functions.…”

mentioning

confidence: 99%

Comparative structural analysis provides new insights into the function of R2‐like ligand‐binding oxidase

et al. 2022

View full text Add to dashboard Cite

R2‐like ligand‐binding oxidase (R2lox) is a ferritin‐like protein that harbours a heterodinuclear manganese–iron active site. Although R2lox function is yet to be established, the enzyme binds a fatty acid ligand coordinating the metal centre and catalyses the formation of a tyrosine–valine ether cross‐link in the protein scaffold upon O2 activation. Here, we characterized the ligands copurified with R2lox by mass spectrometry‐based metabolomics. Moreover, we present the crystal structures of two new homologs of R2lox, from Saccharopolyspora erythraea and Sulfolobus acidocaldarius, at 1.38 Å and 2.26 Å resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.

show abstract

mentioning

confidence: 99%