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PDBsum entry 1rif
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DNA binding protein
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PDB id
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1rif
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of the uvsw helicase from bacteriophage t4.
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Authors
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E.A.Sickmier,
K.N.Kreuzer,
S.W.White.
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Ref.
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Structure, 2004,
12,
583-592.
[DOI no: ]
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PubMed id
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Abstract
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In bacteriophage T4, the WXY system repairs DNA damage by a process that
involves homologous recombination. This system comprises three proteins, the
RecA-like recombination protein UvsX, a recombination mediator protein UvsY, and
a helicase UvsW. Here we report the 2.0 A resolution crystal structure of the
N-terminal two domains of the UvsW helicase (UvsWNF; residues 1-282). The
structure reveals a typical helicase RecA-like domain linked to a small
N-terminal alpha/beta domain that likely binds the nucleic acid substrate. The
missing C-terminal portion of UvsW almost certainly corresponds to the second
RecA-like domain typically found in monomeric helicases. The putative substrate
binding domain is unique within the known helicase structures, and it resembles
the novel "double-wing" DNA binding domain from the phage T4 MotA
transcription factor that mediates the expression of T4 middle genes. The
functional implications of this homology for the role of UvsW in T4 DNA
metabolism are discussed.
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Figure 4.
Figure 4. The UvsW Arginine/Aromatic-Rich Loop(A) A
stereoview showing the conformation of the loop and the
distinctive residues within the loop.(B) A comparison of the
orientations of the loop in molecules A (red) and B (blue) of
the crystal asymmetric unit. The two spheres mark the locations
of the conserved glycine residues that flank the loop. In this
view, the bound dsDNA substrate would be directly below the
loop. The figures were produced using MOLSCRIPT (Kraulis, 1991)
and rendered with RASTER3D (Merritt and Bacon, 1997).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
583-592)
copyright 2004.
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