4LQI

Yeast 20S Proteasome in complex with Vibralactone

Summary for 4LQI

• Entry DOI: 10.2210/pdb4lqi/pdb
• Related: 1RYP 2FAK 3E47
• Descriptor: Proteasome subunit alpha type-2, Proteasome subunit beta type-4, Proteasome subunit beta type-5, ... (16 entities in total)
• Functional Keywords: beta-lactone, inhibitor, natural product, target identification, ntn-protease, cellular protein degradation, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451
• Total number of polymer chains: 28
• Total formula weight: 705047.32

Authors

List, A.,Zeiler, E.,Gallastegui, N.,Rusch, M.,Hedberg, C.,Sieber, S.A.,Groll, M. (deposition date: 2013-07-18, release date: 2013-12-25, Last modification date: 2024-10-30)

Primary citation

List, A.,Zeiler, E.,Gallastegui, N.,Rusch, M.,Hedberg, C.,Sieber, S.A.,Groll, M.
Omuralide and Vibralactone: Differences in the Proteasome-beta-Lactone-gamma-Lactam Binding Scaffold Alter Target Preferences.
Angew.Chem.Int.Ed.Engl., 53:571-574, 2014

PubMed Abstract: Despite their structural similarity, the natural products omuralide and vibralactone have different biological targets. While omuralide blocks the chymotryptic activity of the proteasome with an IC50 value of 47 nM, vibralactone does not have any effect at this protease up to a concentration of 1 mM. Activity-based protein profiling in HeLa cells revealed that the major targets of vibralactone are APT1 and APT2.

PubMed: 24285701
DOI: 10.1002/anie.201308567

Experimental method

X-RAY DIFFRACTION (2.7 Å)