1ul1

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spinqualitylabelsall models 1ul1, resolution 2.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the human FEN1-PCNA complex

Overview

Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic, stability and replication. Proliferating cell nuclear antigen (PCNA) binds, FEN1 and stimulates its endonuclease activity. The structural basis of the, FEN1-PCNA interaction was revealed by the crystal structure of the complex, between human FEN1 and PCNA. The main interface involves the C-terminal, tail of FEN1, which forms two beta-strands connected by a short helix, the, betaA-alphaA-betaB motif, participating in beta-beta and hydrophobic, interactions with PCNA. These interactions are similar to those previously, observed for the p21CIP1/WAF1 peptide. However, this structure involving, the full-length enzyme has revealed additional interfaces that are, involved in the core domain. The interactions at the interfaces maintain, the enzyme in an inactive 'locked-down' orientation and might be utilized, in rapid DNA-tracking by preserving the central hole of PCNA for sliding, along the DNA. A hinge region present between the core domain and the, C-terminal tail of FEN1 would play a role in switching the FEN1, orientation from an inactive to an active orientation.

About this Structure

1UL1 is a Protein complex structure of sequences from Homo sapiens with MG as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for recruitment of human flap endonuclease 1 to PCNA., Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, Fukuda K, Uchida M, Ohtsuka E, Morioka H, Hakoshima T, EMBO J. 2005 Feb 23;24(4):683-93. Epub 2004 Dec 16. PMID:15616578

Page seeded by OCA on Mon Nov 12 19:36:07 2007