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 1.71&Aring;" /> '''STRUCTURE OF THE ZIN...)
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[[Image:1d0q.gif|left|200px]]<br /><applet load="1d0q" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1d0q, resolution 1.71&Aring;" />
'''STRUCTURE OF THE ZINC-BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS DNA PRIMASE'''<br />
'''STRUCTURE OF THE ZINC-BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS DNA PRIMASE'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1D0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D0Q OCA].
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1D0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0Q OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Pan, H.]]
[[Category: Pan, H.]]
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[[Category: Wigley, D.B.]]
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[[Category: Wigley, D B.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: dna primase]]
[[Category: dna primase]]
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[[Category: zinc-binding motif]]
[[Category: zinc-binding motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:55:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:39 2008''

Revision as of 10:11, 21 February 2008


1d0q, resolution 1.71Å

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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 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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