spacer

PDBe Entry: 1dml view

CRYSTAL STRUCTURE OF HERPES SIMPLEX UL42 BOUND TO THE C-TERMINUS OF HSV POL
Summary
Header DNA BINDING PROTEIN/TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.7 Å, R-factor: 23.0%, Free R-factor: 28.1%, Spacegroup: P 1 21 1
Released 15/03/2000, deposition: 14/12/1999, last revision: 24/02/2009
Authors Zuccola, H.J.search; Filman, D.J.search; Coen, D.M.search; Hogle, J.M.search
Primary citation The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase.
MOL.CELLsearch vol:5, pag:267-278 (2000) [PubMed ID 10882068 ]search
Keywords herpes simplex virussearch, dna synthesissearch, sliding clampssearch, PCNAsearch, processivitysearch, DNA BINDING PROTEIN/TRANSFERASE COMPLEXsearch
EC 2.7.7.7 ExPASy BRENDA search 3.1.26.4 ExPASy BRENDA search (B D F H)
Organism Human herpesvirus 1(Herpes simplex virus type 1) 10298search(A C E G B D F H)
UniProt DNA polymerase processivity factor (Polymerase accessory protein) (PAP) (DNA-binding protein UL42) P10226search (A C E G)
DNA polymerase (EC 2.7.7.7) P07917search (B D F H)
Related entries 1plq, 1axc, 1b8h
Polymers
Id Name Type UniProt Residues Observed
A, C, E, G DNA POLYMERASE PROCESSIVITY FACTOR Protein P10226 (PAP_HHV11)search
319 86%
B, D, F, H DNA POLYMERASE Protein P07917 (DPOL_HHV1A)search
36 100%
spacer