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| | <StructureSection load='7kq5' size='340' side='right'caption='[[7kq5]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='7kq5' size='340' side='right'caption='[[7kq5]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7kq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KQ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7kq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KQ5 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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0785 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=7kq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kq5 OCA], [https://pdbe.org/7kq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kq5 RCSB], [https://www.ebi.ac.uk/pdbsum/7kq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kq5 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=7kq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kq5 OCA], [https://pdbe.org/7kq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kq5 RCSB], [https://www.ebi.ac.uk/pdbsum/7kq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kq5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MARIT_THEMA MARIT_THEMA]] Protease that exhibits activity toward chymotrypsin and trypsin substrates. May have antibacterial activity.
| + | [https://www.uniprot.org/uniprot/ENCAP_THEMA ENCAP_THEMA] Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein Flp (ferritin-like protein, may store iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein (PubMed:19172747, PubMed:27224728, PubMed:32961724, PubMed:30376298, PubMed:33769792, PubMed:33953921, PubMed:34815415). Fe(2+) may be able to pass though the 5-fold and dimer channels in the protein shell (Probable).<ref>PMID:19172747</ref> <ref>PMID:27224728</ref> <ref>PMID:30376298</ref> <ref>PMID:32961724</ref> <ref>PMID:33769792</ref> <ref>PMID:33953921</ref> <ref>PMID:34815415</ref> <ref>PMID:33953921</ref> Protease that exhibits activity toward chymotrypsin and trypsin substrates (PubMed:9872409, PubMed:11210524). Probably does not have antibacterial activity (Probable).<ref>PMID:11210524</ref> <ref>PMID:9872409</ref> <ref>PMID:19172747</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Protein nanocompartments are widespread in bacteria and archaea, but their functions are not yet well understood. Here, the cryo-EM structure of a nanocompartment from the thermophilic bacterium Thermotoga maritima is reported at 2.0 A resolution. The high resolution of this structure shows that interactions in the E-loop domain may be important for the thermostability of the nanocompartment assembly. Also, the channels at the fivefold axis, threefold axis and dimer interface are assessed for their ability to transport iron. Finally, an unexpected flavin ligand was identified on the exterior of the shell, indicating that this nanocompartment may also play a direct role in iron metabolism.
| + | |
| - | | + | |
| - | Cryo-EM structure of a thermostable bacterial nanocompartment.,Wiryaman T, Toor N IUCrJ. 2021 Apr 2;8(Pt 3):342-350. doi: 10.1107/S2052252521001949. eCollection, 2021 May 1. PMID:33953921<ref>PMID:33953921</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 7kq5" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Toor, N]] | + | [[Category: Toor N]] |
| - | [[Category: Wiryaman, T I]] | + | [[Category: Wiryaman TI]] |
| - | [[Category: Encapsulin]]
| + | |
| - | [[Category: Flavin-binding]]
| + | |
| - | [[Category: Hk97 fold]]
| + | |
| - | [[Category: Icosahedral]]
| + | |
| - | [[Category: Virus like particle]]
| + | |
| Structural highlights
Function
ENCAP_THEMA Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein Flp (ferritin-like protein, may store iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein (PubMed:19172747, PubMed:27224728, PubMed:32961724, PubMed:30376298, PubMed:33769792, PubMed:33953921, PubMed:34815415). Fe(2+) may be able to pass though the 5-fold and dimer channels in the protein shell (Probable).[1] [2] [3] [4] [5] [6] [7] [8] Protease that exhibits activity toward chymotrypsin and trypsin substrates (PubMed:9872409, PubMed:11210524). Probably does not have antibacterial activity (Probable).[9] [10] [11]
References
- ↑ Sutter M, Boehringer D, Gutmann S, Gunther S, Prangishvili D, Loessner MJ, Stetter KO, Weber-Ban E, Ban N. Structural basis of enzyme encapsulation into a bacterial nanocompartment. Nat Struct Mol Biol. 2008 Sep;15(9):939-47. PMID:19172747
- ↑ Cassidy-Amstutz C, Oltrogge L, Going CC, Lee A, Teng P, Quintanilla D, East-Seletsky A, Williams ER, Savage DF. Identification of a Minimal Peptide Tag for in Vivo and in Vitro Loading of Encapsulin. Biochemistry. 2016 Jun 21;55(24):3461-8. PMID:27224728 doi:10.1021/acs.biochem.6b00294
- ↑ Williams EM, Jung SM, Coffman JL, Lutz S. Pore Engineering for Enhanced Mass Transport in Encapsulin Nanocompartments. ACS Synth Biol. 2018 Nov 16;7(11):2514-2517. PMID:30376298 doi:10.1021/acssynbio.8b00295
- ↑ Xiong X, Sun C, Vago FS, Klose T, Zhu J, Jiang W. Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga Maritima Encapsulin Capsid. Biomolecules. 2020 Sep 19;10(9):1342. PMID:32961724 doi:10.3390/biom10091342
- ↑ Jenkins MC, Lutz S. Encapsulin Nanocontainers as Versatile Scaffolds for the Development of Artificial Metabolons. ACS Synth Biol. 2021 Apr 16;10(4):857-869. PMID:33769792 doi:10.1021/acssynbio.0c00636
- ↑ Wiryaman T, Toor N. Cryo-EM structure of a thermostable bacterial nanocompartment. IUCrJ. 2021 Apr 2;8(Pt 3):342-350. doi: 10.1107/S2052252521001949. eCollection, 2021 May 1. PMID:33953921 doi:http://dx.doi.org/10.1107/S2052252521001949
- ↑ LaFrance BJ, Cassidy-Amstutz C, Nichols RJ, Oltrogge LM, Nogales E, Savage DF. The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein. Sci Rep. 2021 Nov 23;11(1):22810. doi: 10.1038/s41598-021-01932-w. PMID:34815415 doi:http://dx.doi.org/10.1038/s41598-021-01932-w
- ↑ Wiryaman T, Toor N. Cryo-EM structure of a thermostable bacterial nanocompartment. IUCrJ. 2021 Apr 2;8(Pt 3):342-350. doi: 10.1107/S2052252521001949. eCollection, 2021 May 1. PMID:33953921 doi:http://dx.doi.org/10.1107/S2052252521001949
- ↑ Hicks PM, Chang LS, Kelly RM. Homomultimeric protease and putative bacteriocin homolog from Thermotoga maritima. Methods Enzymol. 2001;330:455-60. PMID:11210524 doi:10.1016/s0076-6879(01)30397-x
- ↑ Hicks PM, Rinker KD, Baker JR, Kelly RM. Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria. FEBS Lett. 1998 Dec 4;440(3):393-8. PMID:9872409 doi:10.1016/s0014-5793(98)01451-3
- ↑ Sutter M, Boehringer D, Gutmann S, Gunther S, Prangishvili D, Loessner MJ, Stetter KO, Weber-Ban E, Ban N. Structural basis of enzyme encapsulation into a bacterial nanocompartment. Nat Struct Mol Biol. 2008 Sep;15(9):939-47. PMID:19172747
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