1eqn
From Proteopedia
(New page: 200px<br /><applet load="1eqn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqn, resolution 2.9Å" /> '''E.COLI PRIMASE CATALY...) |
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- | [[Image:1eqn.gif|left|200px]]<br /><applet load="1eqn" size=" | + | [[Image:1eqn.gif|left|200px]]<br /><applet load="1eqn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eqn, resolution 2.9Å" /> | caption="1eqn, resolution 2.9Å" /> | ||
'''E.COLI PRIMASE CATALYTIC CORE'''<br /> | '''E.COLI PRIMASE CATALYTIC CORE'''<br /> | ||
==Overview== | ==Overview== | ||
- | Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of | + | Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a approximately 320 residue fragment of Escherichia coli primase, determined at 2.9 A resolution. Central to the catalytic unit is a TOPRIM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity. |
==About this Structure== | ==About this Structure== | ||
- | 1EQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1EQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Donnell, M | + | [[Category: Donnell, M O.]] |
[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: McInerney, P.]] | [[Category: McInerney, P.]] | ||
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[[Category: toprim domain]] | [[Category: toprim domain]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:32 2008'' |
Revision as of 10:30, 21 February 2008
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E.COLI PRIMASE CATALYTIC CORE
Overview
Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a approximately 320 residue fragment of Escherichia coli primase, determined at 2.9 A resolution. Central to the catalytic unit is a TOPRIM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity.
About this Structure
1EQN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases., Podobnik M, McInerney P, O'Donnell M, Kuriyan J, J Mol Biol. 2000 Jul 7;300(2):353-62. PMID:10873470
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