3L3F

Crystal structure of a PFU-PUL domain pair of Saccharomyces cerevisiae Doa1/Ufd3

Summary for 3L3F

• Entry DOI: 10.2210/pdb3l3f/pdb
• Descriptor: Protein DOA1 (2 entities in total)
• Functional Keywords: armadillo-like repeat structure, nucleus, ubl conjugation pathway, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus: P36037
• Total number of polymer chains: 1
• Total formula weight: 40814.12

Authors

Komori, H.,Nishimasu, R.,Kuno, T.,Higuchi, Y. (deposition date: 2009-12-16, release date: 2010-11-24, Last modification date: 2024-10-30)

Primary citation

Nishimasu, R.,Komori, H.,Higuchi, Y.,Nishimasu, H.,Hiroaki, H.
Crystal Structure of a PFU-PUL Domain Pair of Saccharomyces Cerevisiae Doa1/Ufd3
KOBE J.MED.SCI., 56:E125-E139, 2010

PubMed Abstract: Doa1/Ufd3 is involved in ubiquitin (Ub)-dependent cellular processes in Saccharomyces cerevisiae, and consists of WD40, PFU, and PUL domains. Previous studies showed that the PFU and PUL domains interact with Ub and Hse1, and Cdc48, respectively. However, their detailed functional interactions with Doa1 remained elusive. We report the crystal structure of the PFU-PUL domain pair of yeast Doa1 at 1.9 Å resolution. The conserved surface of the PFU domain may be involved in binding to Ub and Hse1. Unexpectedly, the PUL domain consists of an Armadillo (ARM)-like repeat structure. The positively charged concave surface of the PUL domain may bind to the negatively charged C-terminal region of Cdc48. A structural comparison of Doa1 with Ufd2 revealed that they share a similar ARM-like repeat, supporting a model in which Doa1 and Ufd2 compete for Cdc48 binding and may dictate the fate of ubiquitinated proteins in the proteasome pathway.

PubMed: 21063153

Experimental method

X-RAY DIFFRACTION (1.9 Å)