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Literature summary for 3.4.24.3 extracted from

  • Bauer, R.; Janowska, K.; Taylor, K.; Jordan, B.; Gann, S.; Janowski, T.; Latimer, E.C.; Matsushita, O.; Sakon, J.
    Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH (2015), Acta Crystallogr. Sect. D, 71, 565-577.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structures of Ca2+-bound domain apo s2 to 1.4 A and 1.6 A resolution. ColG-derived domains lack surface aromatic residues, suggesting that the domain is less directly involved in interactions with collagen than that in isoform ColH. The domains are extremely stable in the presence of physiological concentrations of Ca2+ Hathewaya histolytica
X-ray crystal structures of Ca2+-bound domains holo s2b to 1.4 A resolution, and holo s2a to 1.9 A resolution, as well as of Ca2+-free apo s2a to 1.8 A resolution. ColH-derived domains exhibit exposed aromatic residues and are found in M9B collagenases with a single collagen-binding domain. The domains are extremely stable in the presence of physiological concentrations of Ca2+ Hathewaya histolytica

Organism

Organism UniProt Comment Textmining
Hathewaya histolytica Q46085 isoform ColH
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Hathewaya histolytica Q9X721 isoform ColG
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Subunits

Subunits Comment Organism
More isoform ColG consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domain s2 and collagen-binding domains s3a and s3b Hathewaya histolytica
More isoform ColH consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domains s2a and s2b and collagen-binding domain s3 Hathewaya histolytica