2XES
Human PatL1 C-terminal domain (loop variant)
Summary for 2XES
| Entry DOI | 10.2210/pdb2xes/pdb |
| Related | 2XEQ 2XER |
| Descriptor | PROTEIN PAT1 HOMOLOG 1, THIOCYANATE ION, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | mrna decapping, p-bodies, rna binding protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm, P-body: Q86TB9 |
| Total number of polymer chains | 2 |
| Total formula weight | 57925.27 |
| Authors | Tritschler, F.,Weichenrieder, O. (deposition date: 2010-05-17, release date: 2010-06-16, Last modification date: 2024-10-23) |
| Primary citation | Braun, J.E.,Tritschler, F.,Haas, G.,Igreja, C.,Truffault, V.,Weichenrieder, O.,Izaurralde, E. The C-Terminal Alpha-Alpha Superhelix of Pat is Required for Mrna Decapping in Metazoa. Embo J., 29:2368-, 2010 Cited by PubMed Abstract: Pat proteins regulate the transition of mRNAs from a state that is translationally active to one that is repressed, committing targeted mRNAs to degradation. Pat proteins contain a conserved N-terminal sequence, a proline-rich region, a Mid domain and a C-terminal domain (Pat-C). We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions. DCP2 and EDC4 binding is enhanced by the P-rich region and does not require LSm1-7. LSm1-7 binding is assisted by the Mid domain and is reduced by the P-rich region. Structural analysis revealed that Pat-C folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. This conserved and basic surface is required for RNA, DCP2, EDC4 and LSm1-7 binding. The multiplicity of interactions mediated by Pat-C suggests that certain of these interactions are mutually exclusive and, therefore, that Pat proteins switch decapping partners allowing transitions between sequential steps in the mRNA decapping pathway. PubMed: 20543818DOI: 10.1038/EMBOJ.2010.124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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