A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop
Inositol pyrophosphates (PP-IPs) regulate immunity and phosphate homeostasis. Here, the authors’ structural dissection of an Arabidopsis thaliana PP-IP phosphatase reveals that substrates drive their own hydrolysis and identifies a highly elusive metaphosphate-like reaction intermediate.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-04-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-29673-y |
| _version_ | 1818012328785870848 |
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| author | Huanchen Wang Lalith Perera Nikolaus Jork Guangning Zong Andrew M. Riley Barry V. L. Potter Henning J. Jessen Stephen B. Shears |
| author_facet | Huanchen Wang Lalith Perera Nikolaus Jork Guangning Zong Andrew M. Riley Barry V. L. Potter Henning J. Jessen Stephen B. Shears |
| author_sort | Huanchen Wang |
| collection | DOAJ |
| description | Inositol pyrophosphates (PP-IPs) regulate immunity and phosphate homeostasis. Here, the authors’ structural dissection of an Arabidopsis thaliana PP-IP phosphatase reveals that substrates drive their own hydrolysis and identifies a highly elusive metaphosphate-like reaction intermediate. |
| first_indexed | 2024-04-14T06:18:53Z |
| format | Article |
| id | doaj.art-80727188fe0e4b42b9d3d714ec578029 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-14T06:18:53Z |
| publishDate | 2022-04-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-80727188fe0e4b42b9d3d714ec5780292022-12-22T02:08:06ZengNature PortfolioNature Communications2041-17232022-04-0113111310.1038/s41467-022-29673-yA structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loopHuanchen Wang0Lalith Perera1Nikolaus Jork2Guangning Zong3Andrew M. Riley4Barry V. L. Potter5Henning J. Jessen6Stephen B. Shears7Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of HealthGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of HealthInstitute of Organic Chemistry, and CIBSS - the Center for Integrative Biological Signaling Studies, University of FreiburgSignal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of HealthDrug Discovery and Medicinal Chemistry, Department of Pharmacology, University of OxfordDrug Discovery and Medicinal Chemistry, Department of Pharmacology, University of OxfordInstitute of Organic Chemistry, and CIBSS - the Center for Integrative Biological Signaling Studies, University of FreiburgSignal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of HealthInositol pyrophosphates (PP-IPs) regulate immunity and phosphate homeostasis. Here, the authors’ structural dissection of an Arabidopsis thaliana PP-IP phosphatase reveals that substrates drive their own hydrolysis and identifies a highly elusive metaphosphate-like reaction intermediate.https://doi.org/10.1038/s41467-022-29673-y |
| spellingShingle | Huanchen Wang Lalith Perera Nikolaus Jork Guangning Zong Andrew M. Riley Barry V. L. Potter Henning J. Jessen Stephen B. Shears A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop Nature Communications |
| title | A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop |
| title_full | A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop |
| title_fullStr | A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop |
| title_full_unstemmed | A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop |
| title_short | A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop |
| title_sort | structural expose of noncanonical molecular reactivity within the protein tyrosine phosphatase wpd loop |
| url | https://doi.org/10.1038/s41467-022-29673-y |
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