4XW3

Crystal structure of the SPRY domain of the human DEAD-box protein DDX1

4XW3 の概要

• エントリーDOI: 10.2210/pdb4xw3/pdb
• 分子名称: ATP-dependent RNA helicase DDX1 (2 entities in total)
• 機能のキーワード: hydrolase, beta-sandwich, insertion domain, dead-box protein, spry domain
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49289.77

構造登録者

Kellner, J.N.,Meinhart, A. (登録日: 2015-01-28, 公開日: 2015-09-09, 最終更新日: 2024-01-10)

主引用文献

Kellner, J.N.,Meinhart, A.
Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.
Acta Crystallogr.,Sect.F, 71:1176-1188, 2015

PubMed Abstract: The human RNA helicase DDX1 in the DEAD-box family plays an important role in RNA processing and has been associated with HIV-1 replication and tumour progression. Whereas previously described DEAD-box proteins have a structurally conserved core, DDX1 shows a unique structural feature: a large SPRY-domain insertion in its RecA-like consensus fold. SPRY domains are known to function as protein-protein interaction platforms. Here, the crystal structure of the SPRY domain of human DDX1 (hDSPRY) is reported at 2.0 Å resolution. The structure reveals two layers of concave, antiparallel β-sheets that stack onto each other and a third β-sheet beneath the β-sandwich. A comparison with SPRY-domain structures from other eukaryotic proteins showed that the general β-sandwich fold is conserved; however, differences were detected in the loop regions, which were identified in other SPRY domains to be essential for interaction with cognate partners. In contrast, in hDSPRY these loop regions are not strictly conserved across species. Interestingly, though, a conserved patch of positive surface charge is found that may replace the connecting loops as a protein-protein interaction surface. The data presented here comprise the first structural information on DDX1 and provide insights into the unique domain architecture of this DEAD-box protein. By providing the structure of a putative interaction domain of DDX1, this work will serve as a basis for further studies of the interaction network within the hetero-oligomeric complexes of DDX1 and of its recruitment to the HIV-1 Rev protein as a viral replication factor.

PubMed: 26323305
DOI: 10.1107/S2053230X15013709

実験手法

X-RAY DIFFRACTION (2 Å)