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PDBsum entry 1bb8
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References listed in PDB file
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Key reference
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Title
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Site-Specific DNA binding using a variation of the double stranded RNA binding motif.
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Authors
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K.M.Connolly,
J.M.Wojciak,
R.T.Clubb.
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Ref.
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Nat Struct Biol, 1998,
5,
546-550.
[DOI no: ]
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PubMed id
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Abstract
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The integrase family of site-specific recombinases catalyze a diverse array of
DNA rearrangements in archaebacteria, eubacteria and yeast. The solution
structure of the DNA binding domain of the integrase protein from the
conjugative transposon Tn916 has been determined using NMR spectroscopy. The
structure provides the first insights into distal site DNA binding by a
site-specific integrase and reveals that the N-terminal domain is structurally
similar to the double stranded RNA binding domain (dsRBD). The results of
chemical shift mapping experiments suggest that the integrase protein interacts
with DNA using residues located on the face of its three stranded beta-sheet.
This surface differs from the proposed RNA binding surface in dsRBDs, suggesting
that different surfaces on the same protein fold can be used to bind DNA and RNA.
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Figure 1.
Figure 1. The Tn916 transposon. Binding sites for the N- and
C-terminal domains of integrase are shown as triangles and
diamonds respectively. Binding sites for the accessory factor
xis are shown as hexagons.
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Figure 4.
Figure 4. Comparison of the structures of a, Int^N domain
(residues Arg 6−Asp 70 ) and b, staufen dsRBD III protein^22.
Homologous secondary structural elements are colored purple.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
546-550)
copyright 1998.
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