7mu1: Difference between revisions

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<StructureSection load='7mu1' size='340' side='right'caption='[[7mu1]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='7mu1' size='340' side='right'caption='[[7mu1]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7mu1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MU1 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MU1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=7mu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mu1 OCA], [https://pdbe.org/7mu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mu1 RCSB], [https://www.ebi.ac.uk/pdbsum/7mu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mu1 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=7mu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mu1 OCA], [https://pdbe.org/7mu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mu1 RCSB], [https://www.ebi.ac.uk/pdbsum/7mu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mu1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/MARIT_THEMA MARIT_THEMA]] Protease that exhibits activity toward chymotrypsin and trypsin substrates. May have antibacterial activity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based 'organelles' found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25-50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure-function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model Thermotoga maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryo-EM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the Thermotoga maritima encapsulin, the decameric cargo protein with fivefold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier-it also plays a significant role in the structure and function of the cargo enzyme.
The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein.,LaFrance BJ, Cassidy-Amstutz C, Nichols RJ, Oltrogge LM, Nogales E, Savage DF Sci Rep. 2021 Nov 23;11(1):22810. doi: 10.1038/s41598-021-01932-w. PMID:34815415<ref>PMID:34815415</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mu1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: LaFrance, B J]]
[[Category: LaFrance BJ]]
[[Category: Nogales, E]]
[[Category: Nogales E]]
[[Category: Savage, D F]]
[[Category: Savage DF]]
[[Category: Bacterial nanocompartment]]
[[Category: Encapsulin]]
[[Category: Encflp]]
[[Category: Ferritin-like protein]]
[[Category: Fmn]]
[[Category: Thermotoga]]
[[Category: Virus like particle]]

Latest revision as of 22:41, 29 May 2024

Thermotoga maritima encapsulin shellThermotoga maritima encapsulin shell

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7mu1, resolution 3.30Å

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OCA
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