1plq

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(New page: 200px<br /><applet load="1plq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1plq, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1plq.gif|left|200px]]<br /><applet load="1plq" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1plq.gif|left|200px]]<br /><applet load="1plq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1plq, resolution 2.3&Aring;" />
caption="1plq, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA'''<br />
'''CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA'''<br />
==Overview==
==Overview==
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The crystal structure of the processivity factor required by eukaryotic, DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S., cerevisiae, has been determined at 2.3 A resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly, associated to form a closed ring. The dimensions and electrostatic, properties of the ring suggest that PCNA encircles duplex DNA, providing a, DNA-bound platform for the attachment of the polymerase. The trimeric PCNA, ring is strikingly similar to the dimeric ring formed by the beta subunit, (processivity factor) of E. coli DNA polymerase III holoenzyme, with which, it shares no significant sequence identity. This structural correspondence, further substantiates the mechanistic connection between eukaryotic and, prokaryotic DNA replication that has been suggested on biochemical, grounds.
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The crystal structure of the processivity factor required by eukaryotic DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 A resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the beta subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds.
==About this Structure==
==About this Structure==
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1PLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PLQ OCA].
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1PLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLQ OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Burgers, P.M.]]
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[[Category: Burgers, P M.]]
[[Category: Gary, S.]]
[[Category: Gary, S.]]
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[[Category: Kong, X.P.]]
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[[Category: Kong, X P.]]
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[[Category: Krishna, T.S.R.]]
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[[Category: Krishna, T S.R.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
[[Category: HG]]
[[Category: HG]]
[[Category: dna-binding]]
[[Category: dna-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:54:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:04 2008''

Revision as of 12:30, 21 February 2008


1plq, resolution 2.3Å

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CRYSTAL STRUCTURE OF THE EUKARYOTIC DNA POLYMERASE PROCESSIVITY FACTOR PCNA

Overview

The crystal structure of the processivity factor required by eukaryotic DNA polymerase delta, proliferating cell nuclear antigen (PCNA) from S. cerevisiae, has been determined at 2.3 A resolution. Three PCNA molecules, each containing two topologically identical domains, are tightly associated to form a closed ring. The dimensions and electrostatic properties of the ring suggest that PCNA encircles duplex DNA, providing a DNA-bound platform for the attachment of the polymerase. The trimeric PCNA ring is strikingly similar to the dimeric ring formed by the beta subunit (processivity factor) of E. coli DNA polymerase III holoenzyme, with which it shares no significant sequence identity. This structural correspondence further substantiates the mechanistic connection between eukaryotic and prokaryotic DNA replication that has been suggested on biochemical grounds.

About this Structure

1PLQ is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA., Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J, Cell. 1994 Dec 30;79(7):1233-43. PMID:8001157

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