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Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44Crystal Structure of the Human Cytomegalovirus DNA Polymerase Subunit, UL44
Structural highlights
Function[VPAP_HCMVA] Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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