2i5o

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Revision as of 20:34, 12 November 2007

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Solution Structure of the Ubiquitin-Binding Zinc Finger (UBZ) Domain of the Human DNA Y-Polymerase Eta

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The ubiquitin-binding zinc finger (UBZ) domain of human DNA Y-family, polymerase (pol) eta is important in the recruitment of the polymerase to, the stalled replication machinery in translesion synthesis. Here, we, report the solution structure of the pol eta UBZ domain and its, interaction with ubiquitin. We show that the UBZ domain adopts a classical, C(2)H(2) zinc-finger structure characterized by a betabetaalpha fold., Nuclear magnetic resonance titration maps the binding interfaces between, UBZ and ubiquitin to the alpha-helix of the UBZ domain and the canonical, hydrophobic surface of ubiquitin defined by residues L8, I44 and V70., Although the UBZ domain binds ubiquitin through a single alpha-helix, in a, manner similar to the inverted ubiquitin-interacting motif, its structure, is distinct from previously characterized ubiquitin-binding domains. The, pol eta UBZ domain represents a novel member of the C(2)H(2) zinc finger, family that interacts with ubiquitin to regulate translesion synthesis.

Disease

Known diseases associated with this structure: Xeroderma pigmentosum, variant type OMIM:[603968]

About this Structure

2I5O is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase eta., Bomar MG, Pai MT, Tzeng SR, Li SS, Zhou P, EMBO Rep. 2007 Mar;8(3):247-51. Epub 2007 Feb 16. PMID:17304240

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