4E5R

Crystal Structure of Frog DGCR8 Dimerization Domain

4E5R の概要

• エントリーDOI: 10.2210/pdb4e5r/pdb
• 関連するPDBエントリー: 3LE4
• 分子名称: MGC78846 protein (2 entities in total)
• 機能のキーワード: dimerization, ww motif, domain swapping, rna binding protein
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6379.33

構造登録者

Guo, F.,Senturia, R.,Laganowsky, A.,Barr, I.,Scheidemantle, B.D. (登録日: 2012-03-14, 公開日: 2013-02-27, 最終更新日: 2024-02-28)

主引用文献

Senturia, R.,Laganowsky, A.,Barr, I.,Scheidemantle, B.D.,Guo, F.
Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.
Plos One, 7:e39688-e39688, 2012

PubMed Abstract: Human DiGeorge Critical Region 8 (DGCR8) is an essential microRNA (miRNA) processing factor that is activated via direct interaction with Fe(III) heme. In order for DGCR8 to bind heme, it must dimerize using a dimerization domain embedded within its heme-binding domain (HBD). We previously reported a crystal structure of the dimerization domain from human DGCR8, which demonstrated how dimerization results in the formation of a surface important for association with heme. Here, in an attempt to crystallize the HBD, we search for DGCR8 homologues and show that DGCR8 from Patiria miniata (bat star) also binds heme. The extinction coefficients (ε) of DGCR8-heme complexes are determined; these values are useful for biochemical analyses and allow us to estimate the heme occupancy of DGCR8 proteins. Additionally, we present the crystal structure of the Xenopus laevis dimerization domain. The structure is very similar to that of human DGCR8. Our results indicate that dimerization and heme binding are evolutionarily conserved properties of DGCR8 homologues not only in vertebrates, but also in at least some invertebrates.

PubMed: 22768307
DOI: 10.1371/journal.pone.0039688

実験手法

X-RAY DIFFRACTION (1.9 Å)