Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein

Acta Crystallographica. Section F, Structural Biology Communications
Julian N Kellner, Anton Meinhart

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 in...Continue Reading

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Citations

May 11, 2018·Biotechnology & Genetic Engineering Reviews·Vanessa Meier-StephensonTrushar R Patel

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Methods Mentioned

BETA
size-exclusion chromatography
dynamic light scattering

Software Mentioned

GUSTAVUS
OmniSIZE
XDS
Coot
FFT
MOLREP
MolProbity
JCSG Core Suites
Phaser
CNS

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