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PDBsum entry 4xw3
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References listed in PDB file
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Key reference
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Title
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Structure of the spry domain of the human RNA helicase ddx1, A putative interaction platform within a dead-Box protein.
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Authors
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J.N.Kellner,
A.Meinhart.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2015,
71,
1176-1188.
[DOI no: ]
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PubMed id
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Abstract
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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.
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