2YMJ
Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.
Summary for 2YMJ
| Entry DOI | 10.2210/pdb2ymj/pdb |
| NMR Information | BMRB: 18782 |
| Descriptor | PROTEIN QUAKING-A (1 entity in total) |
| Functional Keywords | translation, hairpin, qki, star protein |
| Biological source | XENOPUS LAEVIS (AFRICAN CLAWED FROG) |
| Total number of polymer chains | 2 |
| Total formula weight | 12278.30 |
| Authors | Ali, M.,Broadhurst, R.W. (deposition date: 2012-10-09, release date: 2013-10-30, Last modification date: 2024-07-03) |
| Primary citation | Ali, M.,Broadhurst, R.W. Solution Structure of the Qua1 Dimerization Domain of Pxqua, the Xenopus Ortholog of Quaking. Plos One, 8:57345-, 2013 Cited by PubMed Abstract: The STAR protein family member Quaking is essential for early development in vertebrates. For example, in oligodendrocyte cells it regulates the splicing, localization, translation and lifetime of a set of mRNAs that code for crucial components of myelin. The Quaking protein contains three contiguous conserved regions: a QUA1 oligomerization element, followed by a single-stranded RNA binding motif comprising the KH and QUA2 domains. An embryonic lethal point mutation in the QUA1 domain, E48G, is known to affect both the aggregation state and RNA-binding properties of the murine Quaking ortholog (QKI). Here we report the NMR solution structure of the QUA1 domain from the Xenopus laevis Quaking ortholog (pXqua), which forms a dimer composed of two perpendicularly docked α-helical hairpin motifs. Size exclusion chromatography studies of a range of mutants demonstrate that the dimeric state of the pXqua QUA1 domain is stabilized by a network of interactions between side-chains, with significant roles played by an intra-molecular hydrogen bond between Y41 and E72 (the counterpart to QKI E48) and an inter-protomer salt bridge between E72 and R67. These results are compared with recent structural and mutagenesis studies of QUA1 domains from the STAR family members QKI, GLD-1 and Sam68. PubMed: 23520467DOI: 10.1371/JOURNAL.PONE.0057345 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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