5WTQ

Crystal structure of human proteasome-assembling chaperone PAC4

Summary for 5WTQ

• Entry DOI: 10.2210/pdb5wtq/pdb
• Descriptor: Proteasome assembly chaperone 4, NICKEL (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: proteasome assembly chaperone, chaperone, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 56600.02

Authors

Kurimoto, E.,Satoh, T.,Ito, Y.,Ishihara, E.,Tanaka, K.,Kato, K. (deposition date: 2016-12-13, release date: 2017-03-22, Last modification date: 2024-03-20)

Primary citation

Kurimoto, E.,Satoh, T.,Ito, Y.,Ishihara, E.,Okamoto, K.,Yagi-Utsumi, M.,Tanaka, K.,Kato, K.
Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
Protein Sci., 26:1080-1085, 2017

PubMed Abstract: The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not. In the present study, we determined a crystal structure of human PAC4 at 1.90-Å resolution. Our crystallographic data identify a hydrophobic surface that is surrounded by charged residues. The hydrophobic surface is complementary to that of its binding partner, PAC3. The surface also exhibits charge complementarity with the proteasomal α4-5 subunits. This will provide insights into human proteasome-assembling chaperones as potential anticancer drug targets.

PubMed: 28263418
DOI: 10.1002/pro.3153

Experimental method

X-RAY DIFFRACTION (1.9 Å)