7Q4H

A thermostable lipase from Thermoanaerobacter thermohydrosulfuricus in complex with PMSF

Summary for 7Q4H

• Entry DOI: 10.2210/pdb7q4h/pdb
• Descriptor: Hydrolase_4 domain-containing protein, CHLORIDE ION, GLYCEROL, ... (7 entities in total)
• Functional Keywords: alpha/beta hydrolase, hydrolase, thermostable, pmsf
• Biological source: Thermoanaerobacter thermohydrosulfuricus (Clostridium thermohydrosulfuricum); More
• Total number of polymer chains: 2
• Total formula weight: 60004.42

Authors

Pinotsis, N.,Wilmanns, M. (deposition date: 2021-10-30, release date: 2023-05-10, Last modification date: 2024-05-22)

Primary citation

Pinotsis, N.,Kruger, A.,Tomas, N.,Chatziefthymiou, S.D.,Litz, C.,Mortensen, S.A.,Daffe, M.,Marrakchi, H.,Antranikian, G.,Wilmanns, M.
Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex.
Nat Commun, 14:7649-7649, 2023

PubMed Abstract: The identification and characterization of enzyme function is largely lacking behind the rapidly increasing availability of large numbers of sequences and associated high-resolution structures. This is often hampered by lack of knowledge on in vivo relevant substrates. Here, we present a case study of a high-resolution structure of an unusual orphan lipase in complex with an endogenous C18 monoacylglycerol ester reaction intermediate from the expression host, which is insoluble under aqueous conditions and thus not accessible for studies in solution. The data allowed its functional characterization as a prototypic long-chain monoacylglycerol lipase, which uses a minimal lid domain to position the substrate through a hydrophobic tunnel directly to the enzyme's active site. Knowledge about the molecular details of the substrate binding site allowed us to modulate the enzymatic activity by adjusting protein/substrate interactions, demonstrating the potential of our findings for future biotechnology applications.

PubMed: 38012138
DOI: 10.1038/s41467-023-43354-4

Experimental method

X-RAY DIFFRACTION (2.00003223771 Å)