Open, engage, bind, translocate: The multi-level dynamics of bacterial protein translocation.

Tytuł:: Open, engage, bind, translocate: The multi-level dynamics of bacterial protein translocation.
Autorzy:: Chen W; Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA.
Komives EA; Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA. Electronic address: .
Źródło:: Structure (London, England : 1993) [Structure] 2021 Aug 05; Vol. 29 (8), pp. 781-782.
Typ publikacji:: Journal Article; Comment
Język:: English
Imprint Name(s):: Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993-
MeSH Terms:: Bacterial Proteins*/genetics
Bacterial Proteins*/metabolism
Membrane Transport Proteins*/genetics
Membrane Transport Proteins*/metabolism
Adenosine Triphosphatases/metabolism ; Protein Transport ; SEC Translocation Channels/genetics ; SecA Proteins
Substance Nomenclature:: 0 (Bacterial Proteins)
0 (Membrane Transport Proteins)
0 (SEC Translocation Channels)
EC 3.6.1.- (Adenosine Triphosphatases)
EC 7.4.2.4 (SecA Proteins)
Entry Date(s):: Date Created: 20210806 Date Completed: 20210823 Latest Revision: 20210823
Update Code:: 20240105
DOI:: 10.1016/j.str.2021.07.003
PMID:: 34358463
: Czasopismo naukowe

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The bacterial Sec translocase transports unfolded proteins across membranes. In this issue of Structure, Krishnamurthy et al. (2021) report a nexus of conformational dynamics in the translocase motor protein, SecA. Their findings shed light on the Sec activation mechanism and suggest a general role for multi-level dynamics in protein functions.
(Copyright © 2021. Published by Elsevier Ltd.)

Comment on: Structure. 2021 Aug 5;29(8):846-858.e7. (PMID: 33852897)

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