4PQZ
Crystal structure of swt1 C-terminal domain from yeast
Summary for 4PQZ
| Entry DOI | 10.2210/pdb4pqz/pdb |
| Descriptor | Transcriptional protein SWT1 (2 entities in total) |
| Functional Keywords | hepn like fold, transcription |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus : Q12104 |
| Total number of polymer chains | 1 |
| Total formula weight | 19645.99 |
| Authors | Peng, S.X.,Gao, Z.Q.,Liu, Q.S.,Dong, Y.H. (deposition date: 2014-03-05, release date: 2014-12-03, Last modification date: 2024-11-06) |
| Primary citation | Peng, S.,Zhou, K.,Wang, W.,Gao, Z.,Dong, Y.,Liu, Q. High-resolution crystal structure reveals a HEPN domain at the C-terminal region of S. cerevisiae RNA endonuclease Swt1. Biochem.Biophys.Res.Commun., 453:826-832, 2014 Cited by PubMed Abstract: Swt1 is an RNA endonuclease that plays an important role in quality control of nuclear messenger ribonucleoprotein particles (mRNPs) in eukaryotes; however, its structural details remain to be elucidated. Here, we report the crystal structure of the C-terminal (CT) domain of Swt1 from Saccharomyces cerevisiae, which shares common characteristics of higher eukaryotes and prokaryotes nucleotide binding (HEPN) domain superfamily. To study in detail the full-length protein structure, we analyzed the low-resolution architecture of Swt1 in solution using small angle X-ray scattering (SAXS) method. Both the CT domain and middle domain exhibited a good fit upon superimposing onto the molecular envelope of Swt1. Our study provides the necessary structural information for detailed analysis of the functional role of Swt1, and its importance in the process of nuclear mRNP surveillance. PubMed: 25450355DOI: 10.1016/j.bbrc.2014.10.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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