标题:Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease
作者:Bobeica, Silvia C.; Dong, Shi-Hui; Huo, Liujie; Mazo, Nuria; McLaughlin, Martin I.; Jimenez-Oses, Gonzalo; Nair, Satish K.; van der Donk 更多
作者机构:[Bobeica, Silvia C.; Huo, Liujie; McLaughlin, Martin I.; van der Donk, Wilfred A.] Univ Illinois, Dept Chem, Roger Adams Lab, Urbana, IL 61801 USA.; 更多
通讯作者:van der Donk, WA;Nair, SK;van der Donk, WA;Nair, SK;van der Donk, WA
通讯作者地址:[van der Donk, WA]Univ Illinois, Dept Chem, Roger Adams Lab, Urbana, IL 61801 USA;[Nair, SK; van der Donk, WA]Univ Illinois, Dept Biochem, Roger Adams 更多
来源:ELIFE
出版年:2019
卷:8
DOI:10.7554/eLife.42305
摘要:The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 angstrom resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, nonfunctional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria.
收录类别:SCIE
资源类型:期刊论文
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