Cloned (Comment) | Organism |
---|---|
- |
Hathewaya histolytica |
- |
Clostridium tetani |
Crystallization (Comment) | Organism |
---|---|
crystal structures of the collagenase unit of ColG in the presence and absence of the peptidic inhibitor isoamylphosphonyl-Gly-Pro-Ala bound to the active site. Comparison of isoforms ColH, ColT and ColG reveals differences in domain breathing motions and regulatory elements. Calcium and zinc are required for full peptidolytic activity | Hathewaya histolytica |
crystal structures of the peptidase domains of ColH in the presence and absence of the peptidic inhibitor isoamylphosphonyl-Gly-Pro-Ala bound to the active site. In the unliganded ColH structure, the quaternary subdomain dynamics is modulated by an aspartate switch motion that binds to the catalytic zinc. One calcium binding site is in proximity to the catalytic zinc. Both ions are required for full activity. Loops close to the active site serve as characteristic substrate selectivity filter. Comparison of isoforms ColH, ColT and ColG reveals differences in domain breathing motions and regulatory elements. Calcium and zinc are required for full peptidolytic activity | Hathewaya histolytica |
crystal structures of the peptidase domains of ColT in the presence and absence of the peptidic inhibitor isoamylphosphonyl-Gly-Pro-Ala bound to the active site. Comparison of isoforms ColH, ColT and ColG reveals differences in domain breathing motions and regulatory elements. Calcium and zinc are required for full peptidolytic activity | Clostridium tetani |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetani | Q899Y1 | isoform ColT | - |
Clostridium tetani E88 | Q899Y1 | isoform ColT | - |
Hathewaya histolytica | Q46085 | isoform ColH | - |
Hathewaya histolytica | Q9X721 | isoform ColG | - |
Synonyms | Comment | Organism |
---|---|---|
ColT | - |
Clostridium tetani |