7bok: Difference between revisions

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<StructureSection load='7bok' size='340' side='right'caption='[[7bok]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='7bok' size='340' side='right'caption='[[7bok]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</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='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='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>
<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;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0R4G9_MYCS2 A0R4G9_MYCS2]
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&reg;/PubMed&reg;, 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: Mycolicibacterium smegmatis mc2 155]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Peroxidase]]
[[Category: Gong HR]]
[[Category: Gong, H R]]
[[Category: Mu A]]
[[Category: Mu, A]]
[[Category: Rao ZH]]
[[Category: Rao, Z H]]
[[Category: Tang YT]]
[[Category: Tang, Y T]]
[[Category: Wang Q]]
[[Category: Wang, Q]]
[[Category: Cargo protein]]
[[Category: Dodecamer]]
[[Category: Heme-containing enzyme]]
[[Category: Oxidoreductase]]
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