C-terminal region of A. fulgidus FEN-1 complexed with A. fulgidus PCNA

Structural Basis for FEN-1 Substrate Specificity and PCNA-Mediated Activation in DNA Replication and Repair

Proliferating cell nuclear antigen homolog, PCNA

MIDVIMTGELLKTVTRAIVALVSEARIHFLEKGLHSRAVDPANVAMVIVDIPKDSFEVYNIDEEKTIGVDMDRIFDISKS
ISTKDLVELIVEDESTLKVKFGSVEYKVALIDPSAIRKEPRIPELELPAKIVMDAGEFKKAIAAADKISDQVIFRSDKEG
FRIEAKGDVDSIVFHMTETELIEFNGGEARSMFSVDYLKEFCKVAGSGDLLTIHLGTNYPVRLVFELVGGRAKVEYILAP
RIESE

Na/K phosphate, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 293K

crystal structure of a peptide derived from the consensus sequence of the FEN-1 C-terminus complexed with A. fulgidus PCNA

crystal structure of A. fulgidus FEN-1 bound to DNA

synthetic peptide derived from the PCNA-binding motif of afFEN-1

Carried out twinned refinement in CNS, against the least squares residual for hemihedral twinning. The twinning operator is: h,-h-k,-l. The twin fraction is: 0.370
randomly selected in the shells to ensure that twin-related reflections were selected in pairs

The biological assembly is a trimer generated from the monomer in the asymmetric unit by applying the following transformations:
ROTATION:
[-0.5 -0.86603 0]
[0.86603 -0.5 0]
[0 0 1]
TRANSLATION:
86.53304 -0.00002 0.00002

AND

ROTATION:
[-0.5 0.86603 0]
[-0.86603 -0.5 0]
[0 0 1]
TRANSLATION:
43.26651 74.9398 0.00003

beta-zipper, interdomain connecting loop, DNA repair, DNA replication, REPLICATION