JMJD5 is a human arginyl C-3 hydroxylase
Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-03410-w |
| _version_ | 1818841442271887360 |
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| author | Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury |
| author_facet | Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury |
| author_sort | Sarah E. Wilkins |
| collection | DOAJ |
| description | Jumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures. |
| first_indexed | 2024-12-19T04:26:09Z |
| format | Article |
| id | doaj.art-21f08a0de33a4534a7d964a1710edd68 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T04:26:09Z |
| publishDate | 2018-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-21f08a0de33a4534a7d964a1710edd682022-12-21T20:36:00ZengNature PortfolioNature Communications2041-17232018-03-019111210.1038/s41467-018-03410-wJMJD5 is a human arginyl C-3 hydroxylaseSarah E. Wilkins0Md. Saiful Islam1Joan M. Gannon2Suzana Markolovic3Richard J. Hopkinson4Wei Ge5Christopher J. Schofield6Rasheduzzaman Chowdhury7The Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordThe Department of Chemistry, University of OxfordJumonji-C domain containing protein 5 (JMJD5) is essential for animal development but its catalytic activity has remained elusive so far. Here the authors show that human JMJD5 is an arginyl-hydroxylase and present the cofactor, substrate and product bound JMJD5 crystal structures.https://doi.org/10.1038/s41467-018-03410-w |
| spellingShingle | Sarah E. Wilkins Md. Saiful Islam Joan M. Gannon Suzana Markolovic Richard J. Hopkinson Wei Ge Christopher J. Schofield Rasheduzzaman Chowdhury JMJD5 is a human arginyl C-3 hydroxylase Nature Communications |
| title | JMJD5 is a human arginyl C-3 hydroxylase |
| title_full | JMJD5 is a human arginyl C-3 hydroxylase |
| title_fullStr | JMJD5 is a human arginyl C-3 hydroxylase |
| title_full_unstemmed | JMJD5 is a human arginyl C-3 hydroxylase |
| title_short | JMJD5 is a human arginyl C-3 hydroxylase |
| title_sort | jmjd5 is a human arginyl c 3 hydroxylase |
| url | https://doi.org/10.1038/s41467-018-03410-w |
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