- Abstract:
-
With functions that range from cell envelope structure to signal transduction and transport, lipoproteins constitute 2 to 3% of bacterial genomes and play critical roles in bacterial physiology, pathogenicity, and antibiotic resistance. Lipoproteins are synthesized with a signal peptide securing them to the cytoplasmic membrane with the lipoprotein domain in the periplasm or outside the cell. Posttranslational processing requires a signal peptidase II (LspA) that removes the signal peptide...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1126/science.aad3747
-
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- Funding agency for:
- Stansfeld, PJ
- Publisher:
- American Association for the Advancement of Science Publisher's website
- Journal:
- Science Journal website
- Volume:
- 351
- Issue:
- 6275
- Pages:
- 876-880
- Publication date:
- 2016-02-19
- DOI:
- EISSN:
-
1095-9203
- ISSN:
-
0036-8075
- URN:
-
uuid:6a9f0054-fa33-4302-b99d-d72d6014bb93
- Source identifiers:
-
605635
- Local pid:
- pubs:605635
- Copyright holder:
- Vogeley et al.
- Copyright date:
- 2016
Journal article
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin
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