The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
About this item
Full title
Author / Creator
Markolovic, Suzana , Zhuang, Qinqin , Wilkins, Sarah E. , Eaton, Charlotte D. , Abboud, Martine I. , Katz, Maximiliano J. , McNeil, Helen E. , Leśniak, Robert K. , Hall, Charlotte , Struwe, Weston B. , Konietzny, Rebecca , Davis, Simon , Yang, Ming , Ge, Wei , Benesch, Justin L. P. , Kessler, Benedikt M. , Ratcliffe, Peter J. , Cockman, Matthew E. , Fischer, Roman , Wappner, Pablo , Chowdhury, Rasheduzzaman , Coleman, Mathew L. and Schofield, Christopher J.
Publisher
New York: Nature Publishing Group US
Journal title
Language
English
Formats
Publication information
Publisher
New York: Nature Publishing Group US
Subjects
More information
Scope and Contents
Contents
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (
3S
)
-
lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical and mutation...
Alternative Titles
Full title
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
Authors, Artists and Contributors
Author / Creator
Zhuang, Qinqin
Wilkins, Sarah E.
Eaton, Charlotte D.
Abboud, Martine I.
Katz, Maximiliano J.
McNeil, Helen E.
Leśniak, Robert K.
Hall, Charlotte
Struwe, Weston B.
Konietzny, Rebecca
Davis, Simon
Yang, Ming
Ge, Wei
Benesch, Justin L. P.
Kessler, Benedikt M.
Ratcliffe, Peter J.
Cockman, Matthew E.
Fischer, Roman
Wappner, Pablo
Chowdhury, Rasheduzzaman
Coleman, Mathew L.
Schofield, Christopher J.
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6027965
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6027965
Other Identifiers
ISSN
1552-4450
E-ISSN
1552-4469
DOI
10.1038/s41589-018-0071-y
