7kq5
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== 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/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 == | ||
| + | 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/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:25, 19 May 2021
Cryo-EM structure of a thermostable encapsulin from T. maritima
| |||||||||||
