2GW6
NMR structure of the human tRNA endonuclease SEN15 subunit
Summary for 2GW6
| Entry DOI | 10.2210/pdb2gw6/pdb |
| NMR Information | BMRB: 6860 |
| Descriptor | tRNA-splicing endonuclease subunit Sen15 (1 entity in total) |
| Functional Keywords | sen15_human, trna endonuclease, structural genomics, psi, protein structure initiative, center for eukaryotic structural genomics, cesg, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus (Probable): Q8WW01 |
| Total number of polymer chains | 2 |
| Total formula weight | 27571.51 |
| Authors | Song, J.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-05-03, release date: 2006-05-16, Last modification date: 2024-05-29) |
| Primary citation | Song, J.,Markley, J.L. Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold. J.Mol.Biol., 366:155-164, 2007 Cited by PubMed Abstract: Splicing of eukaryal intron-containing tRNAs requires the action of the heterotetrameric splicing endonuclease, which is composed of two catalytic subunits, Sen34 and Sen2, and two structural subunits, Sen15 and Sen54. Here we report the solution structure of the human tRNA splicing endonuclease subunit HsSen15. To facilitate the structure determination, we removed the disordered 35 N-terminal and 14 C-terminal residues of the full-length protein to produce HsSen15(36-157). The structure of HsSen15(36-157), the first for a subunit of a eukaryal splicing endonuclease, revealed that the protein possesses a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet, arranged in a topology similar to that of the C-terminal domain of Methanocaldococcus jannaschii endonuclease. The dimeric interface is dominated by a beta-barrel structure, formed by face-to-face packing of two, three-stranded beta-sheets. Each of the beta-sheets results from reciprocal parallel pairing of one beta-strand from one subunit with two other beta-strands from the symmetric subunit. The structural model provides insights into the functional assembly of the human tRNA splicing endonuclease. PubMed: 17166513DOI: 10.1016/j.jmb.2006.11.024 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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