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@article{1834740, author = {Cesle, E.E. and Filimoněnko, Anatolij and Tars, K. and Kalnins, G.}, article_location = {HOBOKEN}, article_number = {5}, doi = {http://dx.doi.org/10.1002/pro.4069}, keywords = {bacterial microcompartments; cryo‐ EM; GRM2; Klebsiella pneumoniae}, language = {eng}, issn = {0961-8368}, journal = {Protein Science}, title = {Variety of size and form of GRM2 bacterial microcompartment particles}, url = {https://onlinelibrary.wiley.com/doi/10.1002/pro.4069}, volume = {30}, year = {2021} }
TY - JOUR ID - 1834740 AU - Cesle, E.E. - Filimoněnko, Anatolij - Tars, K. - Kalnins, G. PY - 2021 TI - Variety of size and form of GRM2 bacterial microcompartment particles JF - Protein Science VL - 30 IS - 5 SP - 1035-1043 EP - 1035-1043 PB - JOHN WILEY & SONS INC SN - 09618368 KW - bacterial microcompartments KW - cryo‐ EM KW - GRM2 KW - Klebsiella pneumoniae UR - https://onlinelibrary.wiley.com/doi/10.1002/pro.4069 N2 - Bacterial microcompartments (BMCs) are bacterial organelles involved in enzymatic processes, such as carbon fixation, choline, ethanolamine and propanediol degradation, and others. Formed of a semi-permeable protein shell and an enzymatic core, they can enhance enzyme performance and protect the cell from harmful intermediates. With the ability to encapsulate non-native enzymes, BMCs show high potential for applied use. For this goal, a detailed look into shell form variability is significant to predict shell adaptability. Here we present four novel 3D cryo-EM maps of recombinant Klebsiella pneumoniae GRM2 BMC shell particles with the resolution in range of 9 to 22 angstrom and nine novel 2D classes corresponding to discrete BMC shell forms. These structures reveal icosahedral, elongated, oblate, multi-layered and polyhedral traits of BMCs, indicating considerable variation in size and form as well as adaptability during shell formation processes. ER -
CESLE, E.E., Anatolij FILIMONĚNKO, K. TARS and G. KALNINS. Variety of size and form of GRM2 bacterial microcompartment particles. \textit{Protein Science}. HOBOKEN: JOHN WILEY \&{}amp; SONS INC, 2021, vol.~30, No~5, p.~1035-1043. ISSN~0961-8368. Available from: https://dx.doi.org/10.1002/pro.4069.
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