8WOL
Cryo-EM structure of the Mmp1 encapasulin from Mycobacterium smegmatis
This is a non-PDB format compatible entry.
Summary for 8WOL
| Entry DOI | 10.2210/pdb8wol/pdb |
| EMDB information | 37691 |
| Descriptor | Major membrane protein 1 (1 entity in total) |
| Functional Keywords | mmp1 encapasulin, structural protein |
| Biological source | Mycolicibacterium smegmatis |
| Total number of polymer chains | 60 |
| Total formula weight | 2093107.74 |
| Authors | |
| Primary citation | Tang, Y.,Liu, Y.,Zhang, M.,Lan, W.,Ma, M.,Chen, C.,Wu, S.,Chen, R.,Yan, Y.,Feng, L.,Li, Y.,Guddat, L.W.,Gao, Y.,Liu, X.,Rao, Z. The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin. Commun Biol, 7:1656-1656, 2024 Cited by PubMed Abstract: 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 mc155. 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. PubMed: 39702509DOI: 10.1038/s42003-024-07299-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
Download full validation report






