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-Structure paper
タイトル | Bacteriophage protein PEIP is a potent Bacillus subtilis enolase inhibitor. |
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ジャーナル・号・ページ | Cell Rep, Vol. 40, Issue 1, Page 111026, Year 2022 |
掲載日 | 2022年7月5日 |
![]() | Kaining Zhang / Shanshan Li / Yawen Wang / Zhihao Wang / Nancy Mulvenna / Hang Yang / Peipei Zhang / Huan Chen / Yan Li / Hongliang Wang / Yongxiang Gao / Sivaramesh Wigneshweraraj / Steve Matthews / Kaiming Zhang / Bing Liu / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-33300, PDB-7xml: |
化合物 | ![]() ChemComp-MG: |
由来 |
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![]() | LYASE/LYASE INHIBITOR / Enolase inhibitor / Glycolysis / Bacteriophage / ANTIMICROBIAL PROTEIN / LYASE-LYASE INHIBITOR complex |