1DML

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

Summary for 1DML

• Entry DOI: 10.2210/pdb1dml/pdb
• Related: 1axc 1b8h 1plq
• Descriptor: DNA POLYMERASE PROCESSIVITY FACTOR, DNA POLYMERASE (2 entities in total)
• Functional Keywords: herpes simplex virus, dna synthesis, sliding clamps, pcna, processivity, dna binding protein-transferase complex, dna binding protein/transferase
• Biological source: Human herpesvirus 1 (Herpes simplex virus type 1); More
• Cellular location: Host nucleus: P10226 P07917
• Total number of polymer chains: 8
• Total formula weight: 151932.30

Authors

Zuccola, H.J.,Filman, D.J.,Coen, D.M.,Hogle, J.M. (deposition date: 1999-12-14, release date: 2000-03-15, Last modification date: 2024-02-07)

Primary citation

Zuccola, H.J.,Filman, D.J.,Coen, D.M.,Hogle, J.M.
The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase.
Mol.Cell, 5:267-278, 2000

PubMed Abstract: 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.

PubMed: 10882068
DOI: 10.1016/S1097-2765(00)80422-0

Experimental method

X-RAY DIFFRACTION (2.7 Å)