9y8p

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, probably stores 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:30376298, PubMed:32961724, PubMed:33769792, PubMed:33953921, PubMed:34815415, PubMed:35119930). Fe(2+) may be able to pass though the 5-fold and dimer channels in the protein shell (Probable) (PubMed:33953921).^{[1] [2] [3] [4] [5] [6] [7] [8] [9]} Protease that exhibits activity toward chymotrypsin and trypsin substrates (PubMed:11210524, PubMed:9872409). Probably does not have antibacterial activity (Probable).^{[10] [11] [12]}

References

1. ↑ 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
2. ↑ 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
3. ↑ 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
4. ↑ 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
5. ↑ 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
6. ↑ 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
7. ↑ 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
8. ↑ Adamson LSR, Tasneem N, Andreas MP, Close W, Jenner EN, Szyszka TN, Young R, Cheah LC, Norman A, MacDermott-Opeskin HI, O'Mara ML, Sainsbury F, Giessen TW, Lau YH. Pore structure controls stability and molecular flux in engineered protein cages. Sci Adv. 2022 Feb 4;8(5):eabl7346. doi: 10.1126/sciadv.abl7346. Epub 2022 Feb 4. PMID:35119930 doi:http://dx.doi.org/10.1126/sciadv.abl7346
9. ↑ 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
10. ↑ 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
11. ↑ 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
12. ↑ 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