Literature summary for 3.4.24.3 extracted from

Eckhard, U.; Schoenauer, E.; Nuess, D.; Brandstetter, H.
Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis (2011), Nat. Struct. Mol. Biol., 18, 1109-1114.

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-enzyme, free enzyme and in complex with inhibitor isoamyl-phosphonyl-Gly-Pro-Ala, to 2.55 A, 2.8 A and 3.25 A resolution. Structure shows a distinct segmentation of the N-terminal collagenase module, residues Tyr119-Gly790, forming a saddle-shaped two-domain architecture. The smaller N-terminal saddle flap serves as an activator domain, residues Tyr119-Asp388, and comprises an array of 12 parallel alpha-helices. The catalytic subdomain, residues Asp398-Gln669, adopts a thermolysin-like peptidase fold of mixed alpha and beta type. Leu517-Leu534 form the central helix of the fold and contain the Zn2+-binding 523-HEXXH-527 motif	Hathewaya histolytica

Crystallization (Comment)

Organism

apo-enzyme, free enzyme and in complex with inhibitor isoamyl-phosphonyl-Gly-Pro-Ala, to 2.55 A, 2.8 A and 3.25 A resolution. Structure shows a distinct segmentation of the N-terminal collagenase module, residues Tyr119-Gly790, forming a saddle-shaped two-domain architecture. The smaller N-terminal saddle flap serves as an activator domain, residues Tyr119-Asp388, and comprises an array of 12 parallel alpha-helices. The catalytic subdomain, residues Asp398-Gln669, adopts a thermolysin-like peptidase fold of mixed alpha and beta type. Leu517-Leu534 form the central helix of the fold and contain the Zn2+-binding 523-HEXXH-527 motif

Hathewaya histolytica

Protein Variants

Protein Variants	Comment	Organism
additional information	an activator-deletion construct, containing only the segment Lys396-Lys1118, shows 100% activity against small peptidic substrates as compared to the full-length ColG protease. The peptidase domain alone is completely inactive toward collagen substrates. Full collagenolytic activity is, however, contained in the segment Tyr119-Gly790, comprising the activator and peptidase domains	Hathewaya histolytica

Inhibitors

Inhibitors	Comment	Organism	Structure
isoamyl-phosphonyl-Gly-Pro-Ala	peptidomimetic inhibitor, binds to the edge strand in an antiparallel orientation	Hathewaya histolytica

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the catalytic Zn2+ is tetrahedrally coordinated by the side chains of His523, His527 and Glu555, as well as a water molecule that is further hydrogen-bonded to the general base Glu524	Hathewaya histolytica

Organism

Organism	UniProt	Comment	Textmining
Hathewaya histolytica	Q9X721	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	two-step mechanism in which the N-terminal activator domain cooperates with the peptidase domain in recognition and processing of both collagen triple helices and microfibrils. The activator and peptidase domains remain mostly closed during collagen cleavage but relax to the open ground state once the collagen is degraded, as collagen is the source of the attractive interaction for collagenase closing	Hathewaya histolytica	?	-	?