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Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
DOI:
10.1038/s41598-022-10028-y
Authors:
Rasheduzzaman
Chowdhury
(University of Oxford)
,
Martine I.
Abboud
(University of Oxford)
,
James
Wiley
(University of Oxford)
,
Anthony
Tumber
(University of Oxford)
,
Suzana
Markolovic
(University of Oxford)
,
Christopher J.
Schofield
(University of Oxford)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Scientific Reports
, VOL 12
State:
Published (Approved)
Published:
April 2022
Abstract: The JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1 and 2); JMJD7 has also been reported to have histone endopeptidase activity. Here we report biophysical and biochemical studies on JMJD7 from Drosophila melanogaster (dmJMJD7). Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7). The results further support the assignment of JMJD7 as a lysyl hydroxylase and will help enable the development of selective inhibitors for it and other JmjC oxygenases.
Diamond Keywords: Enzymes
Subject Areas:
Biology and Bio-materials,
Chemistry,
Medicine
Instruments:
I03-Macromolecular Crystallography
,
I04-Macromolecular Crystallography
,
I24-Microfocus Macromolecular Crystallography
Added On:
18/04/2022 21:13
Documents:
s41598-022-10028-y.pdf
Discipline Tags:
Health & Wellbeing
Biochemistry
Chemistry
Structural biology
Drug Discovery
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)