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University of Illinois at Urbana-Champaign
The prlC Suppressor Phenotype and Its Relation to Oligopeptidase a Specificity
Abstract
dc:descriptionComparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Microbiology
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Flores, Theresa M.
- Contributors dc:contributor
-
- Miller, Charles G.
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI3023057
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/86629