Molecular Target Synopsis
Overview
Domains and Structures
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Chemistry
Ligand Efficiency Plot
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colG (Q9X721) - Overview - Molecular Target Synopsis

Protein


colG, Collagenase ColG
Enzyme Classification 3.4.24.3
UniProt Q9X721

Also Known as COLG_HATHI, colG

Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (PubMed:3002446). Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin (PubMed:9922257). The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin (PubMed:9922257). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed (PubMed:21947205, PubMed:23703618). Binding of collagen requires Ca(2+) and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region (PubMed:11121400). Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues (PubMed:11913772).

5IKU
CRYSTAL STRUCTURE OF THE CLOSTRIDIUM HISTOLYTICUM COLG TANDEM COLLAGEN-BINDING DOMAIN S3AS3B IN THE PRESENCE OF CALCIUM AT 1.9 ANGSTROM RESOLUTION
RCSB/PDB
Inspect Structure
See all 3D Structures for colG

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform

Sub-cellular localization


UniProt: colG is active in the following subcellular-locations: secreted.
GO terms: colG is active in the following subcellular-locations: extracellular region.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project colG has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For colG there are:
13 structures (20 chains) solved
2 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis