Molecular architecture and ligand recognition determinants for T4 RNA ligase.
RNA ligase type 1 from bacteriophage T4 (Rnl1) is involved in countering a host defense mechanism by repairing 5'-PO4 and 3'-OH groups in tRNA(Lys). Rnl1 is widely used as a reagent in molecular biology. Although many structures for DNA ligases are available, only fragments of RNA ligases...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2006
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| _version_ | 1826277599694815232 |
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| author | El Omari, K Ren, J Bird, L Bona, M Klarmann, G LeGrice, S Stammers, D |
| author_facet | El Omari, K Ren, J Bird, L Bona, M Klarmann, G LeGrice, S Stammers, D |
| author_sort | El Omari, K |
| collection | OXFORD |
| description | RNA ligase type 1 from bacteriophage T4 (Rnl1) is involved in countering a host defense mechanism by repairing 5'-PO4 and 3'-OH groups in tRNA(Lys). Rnl1 is widely used as a reagent in molecular biology. Although many structures for DNA ligases are available, only fragments of RNA ligases such as Rnl2 are known. We report the first crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate) (AMPcPP). The N-terminal domain is related to the equivalent region of DNA ligases and Rnl2 and binds AMPcPP but with further interactions from the additional N-terminal 70 amino acids in Rnl1 (via Tyr37 and Arg54) and the C-terminal domain (Gly269 and Asp272). The active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism. The C-terminal domain represents a new all alpha-helical fold and has a charge distribution and architecture for helix-nucleic acid groove interaction compatible with tRNA binding. |
| first_indexed | 2024-03-06T23:31:20Z |
| format | Journal article |
| id | oxford-uuid:6c20cd89-270c-4e9e-91fe-db5e7b467695 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:31:20Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:6c20cd89-270c-4e9e-91fe-db5e7b4676952022-03-26T19:08:46ZMolecular architecture and ligand recognition determinants for T4 RNA ligase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6c20cd89-270c-4e9e-91fe-db5e7b467695EnglishSymplectic Elements at Oxford2006El Omari, KRen, JBird, LBona, MKlarmann, GLeGrice, SStammers, DRNA ligase type 1 from bacteriophage T4 (Rnl1) is involved in countering a host defense mechanism by repairing 5'-PO4 and 3'-OH groups in tRNA(Lys). Rnl1 is widely used as a reagent in molecular biology. Although many structures for DNA ligases are available, only fragments of RNA ligases such as Rnl2 are known. We report the first crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate) (AMPcPP). The N-terminal domain is related to the equivalent region of DNA ligases and Rnl2 and binds AMPcPP but with further interactions from the additional N-terminal 70 amino acids in Rnl1 (via Tyr37 and Arg54) and the C-terminal domain (Gly269 and Asp272). The active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism. The C-terminal domain represents a new all alpha-helical fold and has a charge distribution and architecture for helix-nucleic acid groove interaction compatible with tRNA binding. |
| spellingShingle | El Omari, K Ren, J Bird, L Bona, M Klarmann, G LeGrice, S Stammers, D Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title | Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title_full | Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title_fullStr | Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title_full_unstemmed | Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title_short | Molecular architecture and ligand recognition determinants for T4 RNA ligase. |
| title_sort | molecular architecture and ligand recognition determinants for t4 rna ligase |
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