1dml

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(New page: 200px<br /><applet load="1dml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dml, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1dml.gif|left|200px]]<br /><applet load="1dml" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dml, resolution 2.70&Aring;" />
caption="1dml, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL'''<br />
'''CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL'''<br />
==Overview==
==Overview==
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Herpes simplex virus DNA polymerase is a heterodimer composed of a, catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal, structure of a complex of the C-terminal 36 residues of Pol bound to, residues 1-319 of UL42 reveals remarkable similarities between UL42 and, PCNA despite contrasting biochemical properties and lack of sequence, homology. Moreover, the Pol-UL42 interaction resembles the interaction, between the cell cycle regulator p21 and PCNA. The structure and previous, data suggest that the UL42 monomer interacts with DNA quite differently, than does multimeric toroidal PCNA. The details of the structure lead to a, model for the mechanism of UL42, provide the basis for drug design, and, allow modeling of other proteins that lack sequence homology with UL42 or, PCNA.
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Herpes simplex virus DNA polymerase is a heterodimer composed of a catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal structure of a complex of the C-terminal 36 residues of Pol bound to residues 1-319 of UL42 reveals remarkable similarities between UL42 and PCNA despite contrasting biochemical properties and lack of sequence homology. Moreover, the Pol-UL42 interaction resembles the interaction between the cell cycle regulator p21 and PCNA. The structure and previous data suggest that the UL42 monomer interacts with DNA quite differently than does multimeric toroidal PCNA. The details of the structure lead to a model for the mechanism of UL42, provide the basis for drug design, and allow modeling of other proteins that lack sequence homology with UL42 or PCNA.
==About this Structure==
==About this Structure==
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1DML is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. 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=1DML OCA].
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1DML is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. 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=1DML OCA].
==Reference==
==Reference==
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[[Category: Human herpesvirus 4]]
[[Category: Human herpesvirus 4]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Coen, D.M.]]
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[[Category: Coen, D M.]]
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[[Category: Filman, D.J.]]
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[[Category: Filman, D J.]]
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[[Category: Hogle, J.M.]]
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[[Category: Hogle, J M.]]
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[[Category: Zuccola, H.J.]]
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[[Category: Zuccola, H J.]]
[[Category: dna synthesis]]
[[Category: dna synthesis]]
[[Category: herpes simplex virus]]
[[Category: herpes simplex virus]]
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[[Category: sliding clamps]]
[[Category: sliding clamps]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:24:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:17 2008''

Revision as of 10:18, 21 February 2008


1dml, resolution 2.70Å

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CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL

Overview

Herpes simplex virus DNA polymerase is a heterodimer composed of a catalytic subunit, Pol, and an unusual processivity subunit, UL42, which, unlike processivity factors such as PCNA, directly binds DNA. The crystal structure of a complex of the C-terminal 36 residues of Pol bound to residues 1-319 of UL42 reveals remarkable similarities between UL42 and PCNA despite contrasting biochemical properties and lack of sequence homology. Moreover, the Pol-UL42 interaction resembles the interaction between the cell cycle regulator p21 and PCNA. The structure and previous data suggest that the UL42 monomer interacts with DNA quite differently than does multimeric toroidal PCNA. The details of the structure lead to a model for the mechanism of UL42, provide the basis for drug design, and allow modeling of other proteins that lack sequence homology with UL42 or PCNA.

About this Structure

1DML is a Protein complex structure of sequences from Human herpesvirus 4. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase., Zuccola HJ, Filman DJ, Coen DM, Hogle JM, Mol Cell. 2000 Feb;5(2):267-78. PMID:10882068

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