8WT1

Crystal structure of S9 carboxypeptidase from Geobacillus sterothermophilus

Summary for 8WT1

• Entry DOI: 10.2210/pdb8wt1/pdb
• Descriptor: S9 family peptidase, SULFATE ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: carboxypeptidase, prolyl oligopeptidase, oligomerization, acylaminoacyl., hydrolase
• Biological source: Geobacillus stearothermophilus ATCC 12980
• Total number of polymer chains: 8
• Total formula weight: 627525.53

Authors

Chandravanshi, K.,Kumar, A.,Sen, C.,Singh, R.,Bhange, G.B.,Makde, R.D. (deposition date: 2023-10-17, release date: 2024-03-13, Last modification date: 2024-04-10)

Primary citation

Chandravanshi, K.,Singh, R.,Bhange, G.N.,Kumar, A.,Yadav, P.,Kumar, A.,Makde, R.D.
Crystal structure and solution scattering of Geobacillus stearothermophilus S9 peptidase reveal structural adaptations for carboxypeptidase activity.
Febs Lett., 598:684-701, 2024

PubMed Abstract: Acylaminoacyl peptidases (AAPs) play a pivotal role in various pathological conditions and are recognized as potential therapeutic targets. AAPs exhibit a wide range of activities, such as acylated amino acid-dependent aminopeptidase, endopeptidase, and less studied carboxypeptidase activity. We have determined the crystal structure of an AAP from Geobacillus stearothermophilus (S9gs) at 2.0 Å resolution. Despite being annotated as an aminopeptidase in the NCBI database, our enzymatic characterization proved S9gs to be a carboxypeptidase. Solution-scattering studies showed that S9gs exists as a tetramer in solution, and crystal structure analysis revealed adaptations responsible for the carboxypeptidase activity of S9gs. The findings present a hypothesis for substrate selection, substrate entry, and product exit from the active site, enriching our understanding of this rare carboxypeptidase.

PubMed: 38426217
DOI: 10.1002/1873-3468.14834

Experimental method

X-RAY DIFFRACTION (2 Å)