CPDadh: A new peptidase family homologous to the cysteine protease domain in bacterial MARTX toxins
| Autor: | K. Christopher Garcia, Jimin Pei, Patrick J. Lupardus, Nick V. Grishin |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Clostridioides difficile
Protein Conformation Cell adhesion molecule Bacterial Toxins Molecular Sequence Data NASAL EMBRYONIC LHRH FACTOR Sequence alignment Biology biology.organism_classification Biochemistry Cysteine protease Protein Structure Tertiary Microbiology Cysteine Endopeptidases Protein structure Bacterial Proteins Structural Homology Protein For the Record Amino Acid Sequence Sequence Alignment Molecular Biology Peptide sequence Bacteria Cysteine |
| Zdroj: | Protein Science. |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.78 |
| Popis: | A cysteine protease domain (CPD) has been recently discovered in a group of multifunctional, autoprocessing RTX toxins (MARTX) and Clostridium difficile toxins A and B. These CPDs (referred to as CPDmartx) autocleave the toxins to release domains with toxic effects inside host cells. We report identification and computational analysis of CPDadh, a new cysteine peptidase family homologous to CPDmartx. CPDadh and CPDmartx share a Rossmann-like structural core and conserved catalytic residues. In bacteria, domains of the CPDadh family are present at the N-termini of a diverse group of putative cell-cell interaction proteins and at the C-termini of some RHS (recombination hot spot) proteins. In eukaryotes, catalytically inactive members of the CPDadh family are found in cell surface protein NELF (nasal embryonic LHRH factor) and some putative signaling proteins. |
| Databáze: | OpenAIRE |
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