3K6T

Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans at 2.04 A resolution

3K6T の概要

• エントリーDOI: 10.2210/pdb3k6t/pdb
• 分子名称: Female germline-specific tumor suppressor gld-1 (2 entities in total)
• 機能のキーワード: gld-1, qua1 homodimerization domain, helix-turn-helix motif, hydrophobic homodimer interface, perpendicular stacking of protomers, developmental protein, differentiation, meiosis, oogenesis, rna-binding, translation regulation, protein binding
• 由来する生物種: Caenorhabditis elegans (nematode)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 27547.34

構造登録者

Beuck, C.,Szymczyna, B.R.,Kerkow, D.E.,Carmel, A.B.,Columbus, L.,Stanfield, R.L.,Williamson, J.R. (登録日: 2009-10-09, 公開日: 2010-03-09, 最終更新日: 2024-02-21)

主引用文献

Beuck, C.,Szymczyna, B.R.,Kerkow, D.E.,Carmel, A.B.,Columbus, L.,Stanfield, R.L.,Williamson, J.R.
Structure of the GLD-1 homodimerization domain: insights into STAR protein-mediated translational regulation.
Structure, 18:377-389, 2010

PubMed Abstract: Posttranscriptional regulation of gene expression is an important mechanism for modulating protein levels in eukaryotes, especially in developmental pathways. The highly conserved homodimeric STAR/GSG proteins play a key role in regulating translation by binding bipartite consensus sequences in the untranslated regions of target mRNAs, but the exact mechanism remains unknown. Structures of STAR protein RNA binding subdomains have been determined, but structural information is lacking for the homodimerization subdomain. Here, we present the structure of the C. elegans GLD-1 homodimerization domain dimer, determined by a combination of X-ray crystallography and NMR spectroscopy, revealing a helix-turn-helix monomeric fold with the two protomers stacked perpendicularly. Structure-based mutagenesis demonstrates that the dimer interface is not easily disrupted, but the structural integrity of the monomer is crucial for GLD-1 dimerization. Finally, an improved model for STAR-mediated translational regulation of mRNA, based on the GLD-1 homodimerization domain structure, is presented.

PubMed: 20223220
DOI: 10.1016/j.str.2009.12.016

実験手法

X-RAY DIFFRACTION (2.04 Å)