8SW0

Puromycin sensitive aminopeptidase

Summary for 8SW0

• Entry DOI: 10.2210/pdb8sw0/pdb
• Descriptor: Puromycin-sensitive aminopeptidase, ZINC ION, 1,4-DIETHYLENE DIOXIDE, ... (5 entities in total)
• Functional Keywords: aminopeptidase, zinc metallopeptidase, m1 family, four domains, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 102136.41

Authors

Rodgers, D.W.,Sampath, S. (deposition date: 2023-05-17, release date: 2023-07-26, Last modification date: 2024-05-22)

Primary citation

Madabushi, S.,Chow, K.M.,Song, E.S.,Goswami, A.,Hersh, L.B.,Rodgers, D.W.
Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.
Plos One, 18:e0287086-e0287086, 2023

PubMed Abstract: Puromycin-sensitive aminopeptidase (E.C. 3.4.11.14, UniProt P55786), a zinc metallopeptidase belonging to the M1 family, degrades a number of bioactive peptides as well as peptides released from the proteasome, including polyglutamine. We report the crystal structure of PSA at 2.3 Ǻ. Overall, the enzyme adopts a V-shaped architecture with four domains characteristic of the M1 family aminopeptidases, but it is in a less compact conformation compared to most M1 enzymes of known structure. A microtubule binding sequence is present in a C-terminal HEAT repeat domain of the enzyme in a position where it might serve to mediate interaction with tubulin. In the catalytic metallopeptidase domain, an elongated active site groove lined with aromatic and hydrophobic residues and a large S1 subsite may play a role in broad substrate recognition. The structure with bound polyglutamine shows a possible interacting mode of this peptide, which is supported by mutation.

PubMed: 37440518
DOI: 10.1371/journal.pone.0287086

Experimental method

X-RAY DIFFRACTION (2.301 Å)