HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cue...
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
About this item
Full title
Author / Creator
Publisher
New York: Nature Publishing Group US
Journal title
Language
English
Formats
Publication information
Publisher
New York: Nature Publishing Group US
Subjects
More information
Scope and Contents
Contents
HtrA proteases can switch between active and inactive states to adjust their enzymatic activity to the needs of the cell. Structural and biochemical studies of bacterial DegP show that peptide binding to the PDZ domain of DegP induces the conversion of resting hexameric DegP into active higher-order DegP complexes. A specific protease loop in the 1...
Alternative Titles
Full title
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_754870012
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_754870012
Other Identifiers
ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/nsmb.1840
