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PDBsum entry 1d0q
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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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Structure of the zinc-Binding domain of bacillus stearothermophilus DNA primase.
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Authors
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H.Pan,
D.B.Wigley.
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Ref.
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Structure, 2000,
8,
231-239.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: DNA primases catalyse the synthesis of the short RNA primers that
are required for DNA replication by DNA polymerases. Primases comprise three
functional domains: a zinc-binding domain that is responsible for template
recognition, a polymerase domain, and a domain that interacts with the
replicative helicase, DnaB. RESULTS: We present the crystal structure of the
zinc-binding domain of DNA primase from Bacillus stearothermophilus, determined
at 1.7 A resolution. This is the first high-resolution structural information
about any DNA primase. A model is discussed for the interaction of this domain
with the single-stranded DNA template. CONCLUSIONS: The structure of the DNA
primase zinc-binding domain confirms that the protein belongs to the zinc ribbon
subfamily. Structural comparison with other nucleic acid binding proteins
suggests that the beta sheet of primase is likely to be the DNA-binding surface,
with conserved residues on this surface being involved in the binding and
recognition of DNA.
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Figure 4.
Figure 4. Structural comparison of members of the zinc
ribbon family. (a) TFIIB, (b) TFIIS, (c) RPB9 and (d) DNA
primase P12. The zinc ions are shown as a white ball.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2000,
8,
231-239)
copyright 2000.
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