Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity.
Myotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the cry...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4809516?pdf=render |
| _version_ | 1819075860800471040 |
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| author | Seoung Min Bong Kka-bi Son Seung-Won Yang Jae-Won Park Jea-Won Cho Kyung-Tae Kim Hackyoung Kim Seung Jun Kim Young Jun Kim Byung Il Lee |
| author_facet | Seoung Min Bong Kka-bi Son Seung-Won Yang Jae-Won Park Jea-Won Cho Kyung-Tae Kim Hackyoung Kim Seung Jun Kim Young Jun Kim Byung Il Lee |
| author_sort | Seoung Min Bong |
| collection | DOAJ |
| description | Myotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the crystal structure of human MTMR1. The refined model consists of the Pleckstrin homology (PH)-GRAM and phosphatase (PTP) domains. The overall structure was highly similar to the previously reported MTMR2 structure. Interestingly, two phosphate molecules were coordinated by strictly conserved residues located in the C(X)5R motif of the active site. Additionally, our biochemical studies confirmed the substrate specificity of MTMR1 for PI(3)P and PI(3,5)P2 over other phosphatidylinositol phosphates. Our structural and enzymatic analyses provide insight into the catalytic mechanism and biochemical properties of MTMR1. |
| first_indexed | 2024-12-21T18:32:08Z |
| format | Article |
| id | doaj.art-de1a9dcf97f94756affb723246d7cd24 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T18:32:08Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-de1a9dcf97f94756affb723246d7cd242022-12-21T18:54:15ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01113e015261110.1371/journal.pone.0152611Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity.Seoung Min BongKka-bi SonSeung-Won YangJae-Won ParkJea-Won ChoKyung-Tae KimHackyoung KimSeung Jun KimYoung Jun KimByung Il LeeMyotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the crystal structure of human MTMR1. The refined model consists of the Pleckstrin homology (PH)-GRAM and phosphatase (PTP) domains. The overall structure was highly similar to the previously reported MTMR2 structure. Interestingly, two phosphate molecules were coordinated by strictly conserved residues located in the C(X)5R motif of the active site. Additionally, our biochemical studies confirmed the substrate specificity of MTMR1 for PI(3)P and PI(3,5)P2 over other phosphatidylinositol phosphates. Our structural and enzymatic analyses provide insight into the catalytic mechanism and biochemical properties of MTMR1.http://europepmc.org/articles/PMC4809516?pdf=render |
| spellingShingle | Seoung Min Bong Kka-bi Son Seung-Won Yang Jae-Won Park Jea-Won Cho Kyung-Tae Kim Hackyoung Kim Seung Jun Kim Young Jun Kim Byung Il Lee Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. PLoS ONE |
| title | Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. |
| title_full | Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. |
| title_fullStr | Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. |
| title_full_unstemmed | Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. |
| title_short | Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity. |
| title_sort | crystal structure of human myotubularin related protein 1 provides insight into the structural basis of substrate specificity |
| url | http://europepmc.org/articles/PMC4809516?pdf=render |
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