CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.980 | Threonyl-tRNA Synthetase; Chain A, domain 2 | |
3.30.980.50 |
Domain Context
CATH Clusters
Superfamily | 3.30.980.50 |
Functional Family | Microbial collagenase |
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.
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UniProtKB Entries (1)
Q9X721 |
COLG_HATHI
Hathewaya histolytica
Collagenase ColG
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PDB Structure
PDB | 2Y3U |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure of Collagenase G Reveals a Chew-and -Digest Mechanism of Bacterial Collagenolysis
Nat.Struct.Mol.Biol.
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