7kq5 | pdb_00007kq5
From Proteopedia
Cryo-EM structure of a thermostable encapsulin from T. maritima
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Structural highlights
Function[MARIT_THEMA] Protease that exhibits activity toward chymotrypsin and trypsin substrates. May have antibacterial activity. Publication Abstract from PubMedProtein 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 10:25, 19 May 2021.