1d0q
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(New page: 200px<br /><applet load="1d0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0q, resolution 1.71Å" /> '''STRUCTURE OF THE ZIN...)
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Revision as of 10:47, 20 November 2007
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STRUCTURE OF THE ZINC-BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS DNA PRIMASE
Overview
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.
About this Structure
1D0Q is a Single protein structure of sequence from Geobacillus stearothermophilus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase., Pan H, Wigley DB, Structure. 2000 Mar 15;8(3):231-9. PMID:10745010
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