7XML

Cryo-EM structure of PEIP-Bs_enolase complex

Summary for 7XML

• Entry DOI: 10.2210/pdb7xml/pdb
• EMDB information: 33300
• Descriptor: Enolase, Putative gene 60 protein, MAGNESIUM ION (3 entities in total)
• Functional Keywords: enolase inhibitor, glycolysis, bacteriophage, antimicrobial protein, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• Biological source: Bacillus subtilis (strain 168); More
• Total number of polymer chains: 4
• Total formula weight: 110417.78

Authors

Li, S.,Zhang, K. (deposition date: 2022-04-26, release date: 2022-07-27, Last modification date: 2024-07-03)

Primary citation

Zhang, K.,Li, S.,Wang, Y.,Wang, Z.,Mulvenna, N.,Yang, H.,Zhang, P.,Chen, H.,Li, Y.,Wang, H.,Gao, Y.,Wigneshweraraj, S.,Matthews, S.,Zhang, K.,Liu, B.
Bacteriophage protein PEIP is a potent Bacillus subtilis enolase inhibitor.
Cell Rep, 40:111026-111026, 2022

PubMed Abstract: Enolase is a highly conserved enzyme that presents in all organisms capable of glycolysis or fermentation. Its immediate product phosphoenolpyruvate is essential for other important processes like peptidoglycan synthesis and the phosphotransferase system in bacteria. Therefore, enolase inhibitors are of great interest. Here, we report that Gp60, a phage-encoded enolase inhibitor protein (PEIP) of bacteriophage SPO1 for Bacillus subtilis, is an enolase inhibitor. PEIP-expressing bacteria exhibit growth attenuation, thinner cell walls, and safranin color in Gram staining owing to impaired peptidoglycan synthesis. We solve the structure of PEIP-enolase tetramer and show that PEIP disassembles enolase by disrupting the basic dimer unit. The structure reveals that PEIP does not compete for substrate binding but induces a cascade of conformational changes that limit accessibility to the enolase catalytic site. This phage-inspired disassembly of enolase represents an alternative strategy for the development of anti-microbial drugs.

PubMed: 35793626
DOI: 10.1016/j.celrep.2022.111026

Experimental method

ELECTRON MICROSCOPY (3.2 Å)