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The | ==Cryo-EM structure of the 10-subunits Mmp1 complex from Mycobacterium smegmatis== | ||
<StructureSection load='8won' size='340' side='right'caption='[[8won]], [[Resolution|resolution]] 2.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8won]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WON FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.69Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8won FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8won OCA], [https://pdbe.org/8won PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8won RCSB], [https://www.ebi.ac.uk/pdbsum/8won PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8won ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A653FP42_MYCSM A0A653FP42_MYCSM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A and 2.69 A. The Enc-CD at 2.10 A 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. | |||
The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin.,Tang Y, Liu Y, Zhang M, Lan W, Ma M, Chen C, Wu S, Chen R, Yan Y, Feng L, Li Y, Guddat LW, Gao Y, Liu X, Rao Z Commun Biol. 2024 Dec 19;7(1):1656. doi: 10.1038/s42003-024-07299-8. PMID:39702509<ref>PMID:39702509</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8won" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycolicibacterium smegmatis]] | ||
[[Category: Gao Y]] | |||
[[Category: Lan W]] | |||
[[Category: Liu X]] | |||
[[Category: Liu Y]] | |||
[[Category: Ma M]] | |||
[[Category: Tang Y]] | |||
[[Category: Zhang M]] |
Latest revision as of 16:58, 1 January 2025
Cryo-EM structure of the 10-subunits Mmp1 complex from Mycobacterium smegmatisCryo-EM structure of the 10-subunits Mmp1 complex from Mycobacterium smegmatis
Structural highlights
FunctionPublication Abstract from PubMedEncapsulin 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 A and 2.69 A. The Enc-CD at 2.10 A 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. The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin.,Tang Y, Liu Y, Zhang M, Lan W, Ma M, Chen C, Wu S, Chen R, Yan Y, Feng L, Li Y, Guddat LW, Gao Y, Liu X, Rao Z Commun Biol. 2024 Dec 19;7(1):1656. doi: 10.1038/s42003-024-07299-8. PMID:39702509[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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