Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase

Using a combination of dual covalent crosslinking and cryo-EM analyses, we elucidate the structure of mycocerosic acid synthase from Mycobacterium tuberculosis trapped in two distinct catalytic states during its iterative cycle. These structures reveal domain architecture of the acyl carrier protein...

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Vydané v:	Nature communications Ročník 16; číslo 1; s. 7798 - 14
Hlavní autori:	Jiang, Ziran, Heberlig, Graham W., Chen, Jeffrey A., Huynh, Jennifer, La Clair, James J., Burkart, Michael D.
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 21.08.2025 Nature Publishing Group Nature Portfolio
Predmet:	147/28 631/45 631/535 631/535/1258/1259 631/57 631/92/349 Acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - metabolism Acyl Carrier Protein - ultrastructure Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biosynthesis Catalytic Domain Cross-Linking Reagents - chemistry Crosslinking Cryoelectron Microscopy Dehydration E coli Enzymes Humanities and Social Sciences Models, Molecular multidisciplinary Multidrug resistant organisms Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology Mycobacterium tuberculosis - metabolism Polyketide synthase Polyketide Synthases - chemistry Polyketide Synthases - metabolism Polyketide Synthases - ultrastructure Protein interaction Proteins Science Science (multidisciplinary) Tuberculosis Virulence factors
ISSN:	2041-1723, 2041-1723
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