CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.120 | Jelly Rolls |
|
2.60.120.380 |
Domain Context
CATH Clusters
| Superfamily | 2.60.120.380 |
| Functional Family |
Enzyme Information
| 3.4.24.3 |
Microbial collagenase.
based on mapping to UniProt Q9X721
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
-!- Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. -!- Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). -!- The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. -!- The enzymes also act as peptidyl-tripeptidases. -!- Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus). -!- Also known from Streptomyces sp. -!- Belongs to peptidase family M9. -!- Formerly EC 3.4.4.19, EC 3.4.24.8 and EC 3.4.99.5.
|
UniProtKB Entries (1)
| Q9X721 |
COLG_HATHI
Hathewaya histolytica
Collagenase ColG
|
PDB Structure
| PDB | 1NQJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A bacterial collagen-binding domain with novel calcium-binding motif
controls domain orientation
Embo J.
|
