3WUP

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

Summary for 3WUP

• Entry DOI: 10.2210/pdb3wup/pdb
• Descriptor: DNA polymerase eta, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: ubiquitin-binding zinc finger, zinc finger, ubiquitin and ubiquitin-binding domain, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q9Y253
• Total number of polymer chains: 1
• Total formula weight: 4614.91

Authors

Suzuki, N.,Wakatsuki, S.,Kawasaki, S. (deposition date: 2014-05-01, release date: 2015-06-17, Last modification date: 2024-05-29)

Primary citation

Suzuki, N.,Rohaim, A.,Kato, R.,Dikic, I.,Wakatsuki, S.,Kawasaki, M.
A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1.
Febs J., 283:2004-2017, 2016

PubMed Abstract: The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating β-β-α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. Here, we report the crystal structure of the UBZ domain of Y-family DNA polymerase (pol) η and the crystal structure of the complex between the UBZ domain of Werner helicase-interacting protein 1 (WRNIP1) and ubiquitin, crystallized using the GFP fusion technique. In contrast to the pol η UBZ, which has been proposed to bind ubiquitin via its C-terminal α-helix, ubiquitin binds to a novel surface of WRNIP1 UBZ composed of the first β-strand and the C-terminal α-helix. In addition, we report the structure of the tandem UBZ domains of Tax1-binding protein 1 (TAX1BP1) and show that the second UBZ of TAX1BP1 binds ubiquitin, presumably in a manner similar to that of WRNIP1 UBZ. We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin-binding surfaces: the pol η type and the WRNIP1 type.

PubMed: 27062441
DOI: 10.1111/febs.13734

Experimental method

X-RAY DIFFRACTION (1.6 Å)