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1t6l

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(New page: 200px<br /><applet load="1t6l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6l, resolution 1.85&Aring;" /> '''Crystal Structure of...)
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[[Image:1t6l.jpg|left|200px]]<br /><applet load="1t6l" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1t6l, resolution 1.85&Aring;" />
'''Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44'''<br />
'''Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44'''<br />
==Overview==
==Overview==
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The human cytomegalovirus DNA polymerase consists of a catalytic subunit, UL54, and a presumed processivity factor, UL44. We have solved the crystal, structure of residues 1-290 of UL44 to 1.85 A resolution by, multiwavelength anomalous dispersion. The structure reveals a dimer of, UL44 in the shape of a C clamp. Each monomer of UL44 shares its overall, fold with other processivity factors, including herpes simplex virus UL42, which is a monomer that binds DNA directly, and the sliding clamp, PCNA, which is a trimer that surrounds DNA, although these proteins share no, obvious sequence homology. Analytical ultracentrifugation and gel, filtration measurements demonstrated that UL44 also forms a dimer in, solution, and substitution of large hydrophobic residues along the, homodimer interface with alanine disrupted dimerization and decreased DNA, binding. UL44 represents a hybrid processivity factor as it binds DNA, directly like UL42, but forms a C clamp that may surround DNA like PCNA.
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The human cytomegalovirus DNA polymerase consists of a catalytic subunit, UL54, and a presumed processivity factor, UL44. We have solved the crystal structure of residues 1-290 of UL44 to 1.85 A resolution by multiwavelength anomalous dispersion. The structure reveals a dimer of UL44 in the shape of a C clamp. Each monomer of UL44 shares its overall fold with other processivity factors, including herpes simplex virus UL42, which is a monomer that binds DNA directly, and the sliding clamp, PCNA, which is a trimer that surrounds DNA, although these proteins share no obvious sequence homology. Analytical ultracentrifugation and gel filtration measurements demonstrated that UL44 also forms a dimer in solution, and substitution of large hydrophobic residues along the homodimer interface with alanine disrupted dimerization and decreased DNA binding. UL44 represents a hybrid processivity factor as it binds DNA directly like UL42, but forms a C clamp that may surround DNA like PCNA.
==About this Structure==
==About this Structure==
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1T6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6L OCA].
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1T6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6L OCA].
==Reference==
==Reference==
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[[Category: Human herpesvirus 5]]
[[Category: Human herpesvirus 5]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Appleton, B.A.]]
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[[Category: Appleton, B A.]]
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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.]]
[[Category: Loregian, A.]]
[[Category: Loregian, A.]]
[[Category: processivity fold]]
[[Category: processivity fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:01:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:30 2008''

Revision as of 13:10, 21 February 2008


1t6l, resolution 1.85Å

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Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44

Overview

The human cytomegalovirus DNA polymerase consists of a catalytic subunit, UL54, and a presumed processivity factor, UL44. We have solved the crystal structure of residues 1-290 of UL44 to 1.85 A resolution by multiwavelength anomalous dispersion. The structure reveals a dimer of UL44 in the shape of a C clamp. Each monomer of UL44 shares its overall fold with other processivity factors, including herpes simplex virus UL42, which is a monomer that binds DNA directly, and the sliding clamp, PCNA, which is a trimer that surrounds DNA, although these proteins share no obvious sequence homology. Analytical ultracentrifugation and gel filtration measurements demonstrated that UL44 also forms a dimer in solution, and substitution of large hydrophobic residues along the homodimer interface with alanine disrupted dimerization and decreased DNA binding. UL44 represents a hybrid processivity factor as it binds DNA directly like UL42, but forms a C clamp that may surround DNA like PCNA.

About this Structure

1T6L is a Single protein structure of sequence from Human herpesvirus 5. Full crystallographic information is available from OCA.

Reference

The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer., Appleton BA, Loregian A, Filman DJ, Coen DM, Hogle JM, Mol Cell. 2004 Jul 23;15(2):233-44. PMID:15260974

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