7bok
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Cryo-EM structure of the encapsulated DyP-type peroxidase from Mycobacterium smegmatis== | ==Cryo-EM structure of the encapsulated DyP-type peroxidase from Mycobacterium smegmatis== | ||
| - | <StructureSection load='7bok' size='340' side='right'caption='[[7bok]]' scene=''> | + | <StructureSection load='7bok' size='340' side='right'caption='[[7bok]], [[Resolution|resolution]] 3.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BOK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bok]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_mc2_155 Mycolicibacterium smegmatis mc2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BOK FirstGlance]. <br> |
| - | </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=7bok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bok OCA], [https://pdbe.org/7bok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bok RCSB], [https://www.ebi.ac.uk/pdbsum/7bok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bok ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span></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=7bok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bok OCA], [https://pdbe.org/7bok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bok RCSB], [https://www.ebi.ac.uk/pdbsum/7bok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bok ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Encapsulins containing dye-decolorizing peroxidase (DyP)-type peroxidases are ubiquitous among prokaryotes, protecting cells against oxidative stress. However, little is known about how they interact and function. Here, we have isolated a native cargo-packaging encapsulin from Mycobacterium smegmatis and determined its complete high-resolution structure by cryogenic electron microscopy (cryo-EM). This encapsulin comprises an icosahedral shell and a dodecameric DyP cargo. The dodecameric DyP consists of two hexamers with a twofold axis of symmetry and stretches across the interior of the encapsulin. Our results reveal that the encapsulin shell plays a role in stabilizing the dodecameric DyP. Furthermore, we have proposed a potential mechanism for removing the hydrogen peroxide based on the structural features. Our study also suggests that the DyP is the primary cargo protein of mycobacterial encapsulins and is a potential target for antituberculosis drug discovery. | ||
| + | |||
| + | Cryo-EM structure of Mycobacterium smegmatis DyP-loaded encapsulin.,Tang Y, Mu A, Zhang Y, Zhou S, Wang W, Lai Y, Zhou X, Liu F, Yang X, Gong H, Wang Q, Rao Z Proc Natl Acad Sci U S A. 2021 Apr 20;118(16). pii: 2025658118. doi:, 10.1073/pnas.2025658118. PMID:33853951<ref>PMID:33853951</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7bok" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gong | + | [[Category: Mycolicibacterium smegmatis mc2 155]] |
| - | [[Category: Mu A]] | + | [[Category: Peroxidase]] |
| - | [[Category: Rao | + | [[Category: Gong, H R]] |
| - | [[Category: Tang | + | [[Category: Mu, A]] |
| - | [[Category: Wang Q]] | + | [[Category: Rao, Z H]] |
| + | [[Category: Tang, Y T]] | ||
| + | [[Category: Wang, Q]] | ||
| + | [[Category: Cargo protein]] | ||
| + | [[Category: Dodecamer]] | ||
| + | [[Category: Heme-containing enzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 05:31, 28 April 2021
Cryo-EM structure of the encapsulated DyP-type peroxidase from Mycobacterium smegmatis
| |||||||||||
