The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin

Encapsulin nanocompartments loaded with dedicated cargo proteins via unique targeting peptides, play a key role in stress resistance, iron storage and natural product biosynthesis. Mmp1 and cysteine desulfurase (Enc-CD) have been identified as the most abundant representatives of family 2 encapsulin...

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Vydáno v:	Communications biology Ročník 7; číslo 1; s. 1656 - 14
Hlavní autoři:	Tang, Yanting, Liu, Yanyan, Zhang, Mingjing, Lan, Weiqi, Ma, Mengyuan, Chen, Cheng, Wu, Saibin, Chen, Rong, Yan, Yiran, Feng, Lu, Li, Ying, Guddat, Luke W., Gao, Yan, Liu, Xiang, Rao, Zihe
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 19.12.2024 Nature Publishing Group Nature Portfolio
Témata:	101/28 631/45/535 631/57 82/83 Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bioengineering Biology Biomedical and Life Sciences Biosynthesis Carbon-Sulfur Lyases - chemistry Carbon-Sulfur Lyases - metabolism Conformation Cryoelectron Microscopy Crystal structure Crystallography, X-Ray Cysteine Leprosy Life Sciences Metabolism Models, Molecular Mycobacterium smegmatis Mycobacterium smegmatis - enzymology Mycobacterium smegmatis - metabolism Natural products Oxidation Peptides Physiology Polymerization Protein Conformation Proteins Structure-function relationships Sulfur Therapeutic applications
ISSN:	2399-3642, 2399-3642
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Shrnutí:	Encapsulin nanocompartments loaded with dedicated cargo proteins via unique targeting peptides, play a key role in stress resistance, iron storage and natural product biosynthesis. Mmp1 and cysteine desulfurase (Enc-CD) have been identified as the most abundant representatives of family 2 encapsulin systems. However, the molecular assembly, catalytic mechanism, and physiological functions of the Mmp1 encapsulin system have not been studied in detail. Here we isolate and characterize an Enc-CD-loaded Mmp1 encapsulin system from Mycobacterium smegmatis mc 2 155. The cryo-EM structure of the Mmp1 encapsulin and the crystal structure of the naked cargo Enc-CD have been determined. The structure shows that the Mmp1 protomer assembles two conformation models, the icosahedron ( T = 1) and homodecamer, with the resolution of 2.60 Å and 2.69 Å. The Enc-CD at 2.10 Å resolution is dimeric and loaded into the Mmp1 ( T = 1) encapsulin through the N-terminal long disordered region. Mmp1 encapsulin protects Enc-CD against oxidation as well as to maintain structural stability. These studies provide new insights into the mechanism by which Enc-CD-loaded encapsulin stores sulfur and provides a framework for discovery of new anti-mycobacterial therapeutics. Tang et al. present the isolation and characterization of an Mmp1 encapsulin system from Mycobacterium smegmatis , highlighting its structural and functional features. The study reveals the cryo-EM and crystal structures, offering insights into the role of Enc-CD-loaded encapsulin in sulfur storage, stress resistance, and potential therapeutic applications against mycobacterial infections.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	2399-3642 2399-3642
DOI:	10.1038/s42003-024-07299-8