2YMJ

Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.

2YMJ の概要

• エントリーDOI: 10.2210/pdb2ymj/pdb
• NMR情報: BMRB: 18782
• 分子名称: PROTEIN QUAKING-A (1 entity in total)
• 機能のキーワード: translation, hairpin, qki, star protein
• 由来する生物種: XENOPUS LAEVIS (AFRICAN CLAWED FROG)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12278.30

構造登録者

Ali, M.,Broadhurst, R.W. (登録日: 2012-10-09, 公開日: 2013-10-30, 最終更新日: 2024-07-03)

主引用文献

Ali, M.,Broadhurst, R.W.
Solution Structure of the Qua1 Dimerization Domain of Pxqua, the Xenopus Ortholog of Quaking.
Plos One, 8:57345-, 2013

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: 23520467
DOI: 10.1371/JOURNAL.PONE.0057345

実験手法

SOLUTION NMR