2pol: Difference between revisions

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New page: left|200px<br /><applet load="2pol" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pol, resolution 2.5Å" /> '''THREE-DIMENSIONAL STR...
 
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[[Image:2pol.jpg|left|200px]]<br /><applet load="2pol" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2pol.jpg|left|200px]]<br /><applet load="2pol" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2pol, resolution 2.5&Aring;" />
caption="2pol, resolution 2.5&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF THE BETA SUBUNIT OF ESCHERICHIA COLI DNA POLYMERASE III HOLOENZYME: A SLIDING DNA CLAMP'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF THE BETA SUBUNIT OF ESCHERICHIA COLI DNA POLYMERASE III HOLOENZYME: A SLIDING DNA CLAMP'''<br />


==Overview==
==Overview==
The crystal structure of the beta subunit (processivity factor) of DNA, polymerase III holoenzyme has been determined at 2.5 A resolution. A dimer, of the beta subunit (M(r) = 2 x 40.6 kd, 2 x 366 amino acid residues), forms a ring-shaped structure lined by 12 alpha helices that can encircle, duplex DNA. The structure is highly symmetrical, with each monomer, containing three domains of identical topology. The charge distribution, and orientation of the helices indicate that the molecule functions by, forming a tight clamp that can slide on DNA, as shown biochemically. A, potential structural relationship is suggested between the beta subunit, and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase, delta [and epsilon] processivity factor), and the gene 45 protein of the, bacteriophage T4 DNA polymerase.
The crystal structure of the beta subunit (processivity factor) of DNA polymerase III holoenzyme has been determined at 2.5 A resolution. A dimer of the beta subunit (M(r) = 2 x 40.6 kd, 2 x 366 amino acid residues) forms a ring-shaped structure lined by 12 alpha helices that can encircle duplex DNA. The structure is highly symmetrical, with each monomer containing three domains of identical topology. The charge distribution and orientation of the helices indicate that the molecule functions by forming a tight clamp that can slide on DNA, as shown biochemically. A potential structural relationship is suggested between the beta subunit and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase delta [and epsilon] processivity factor), and the gene 45 protein of the bacteriophage T4 DNA polymerase.


==About this Structure==
==About this Structure==
2POL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2POL OCA].  
2POL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2POL OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kong, X.P.]]
[[Category: Kong, X P.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
[[Category: nucleotidyltransferase]]
[[Category: nucleotidyltransferase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:35 2008''

Revision as of 19:31, 21 February 2008

File:2pol.jpg


2pol, resolution 2.5Å

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THREE-DIMENSIONAL STRUCTURE OF THE BETA SUBUNIT OF ESCHERICHIA COLI DNA POLYMERASE III HOLOENZYME: A SLIDING DNA CLAMP

OverviewOverview

The crystal structure of the beta subunit (processivity factor) of DNA polymerase III holoenzyme has been determined at 2.5 A resolution. A dimer of the beta subunit (M(r) = 2 x 40.6 kd, 2 x 366 amino acid residues) forms a ring-shaped structure lined by 12 alpha helices that can encircle duplex DNA. The structure is highly symmetrical, with each monomer containing three domains of identical topology. The charge distribution and orientation of the helices indicate that the molecule functions by forming a tight clamp that can slide on DNA, as shown biochemically. A potential structural relationship is suggested between the beta subunit and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase delta [and epsilon] processivity factor), and the gene 45 protein of the bacteriophage T4 DNA polymerase.

About this StructureAbout this Structure

2POL is a Single protein structure of sequence from Escherichia coli. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp., Kong XP, Onrust R, O'Donnell M, Kuriyan J, Cell. 1992 May 1;69(3):425-37. PMID:1349852

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