Literature summary for 3.4.24.3 extracted from

Bauer, R.; Wilson, J.J.; Philominathan, S.T.; Davis, D.; Matsushita, O.; Sakon, J.
Structural comparison of ColH and ColG collagen-binding domains from Clostridium histolyticum (2013), J. Bacteriol., 195, 318-327.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of ColG collagen-binding domain s3b, to 2.0 A resolution. All but one residue, whose side chain chelates with Ca2+, are conserved	Hathewaya histolytica
crystal structures of ColH collagen-binding domain, to 2.0 A resolution. All but one residue, whose side chain chelates with Ca2+, are conserved. The dual Ca2+ binding site in s3 is completed by an unconserved aspartate. Domain s3 gains thermal stability, comparable to domain s3b of isoform ColG, by binding to Ca2+. holo s3 is also stabilized against chemical denaturants urea and guanidine HCl. The general shape of the binding pocket is retained by altered loop structures and side chain positions. Domain s3 also binds asymmetrically to minicollagen	Hathewaya histolytica

Crystallization (Comment)

Organism

crystal structure of ColG collagen-binding domain s3b, to 2.0 A resolution. All but one residue, whose side chain chelates with Ca2+, are conserved

Hathewaya histolytica

crystal structures of ColH collagen-binding domain, to 2.0 A resolution. All but one residue, whose side chain chelates with Ca2+, are conserved. The dual Ca2+ binding site in s3 is completed by an unconserved aspartate. Domain s3 gains thermal stability, comparable to domain s3b of isoform ColG, by binding to Ca2+. holo s3 is also stabilized against chemical denaturants urea and guanidine HCl. The general shape of the binding pocket is retained by altered loop structures and side chain positions. Domain s3 also binds asymmetrically to minicollagen

Hathewaya histolytica

Organism

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

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
70.2	-	melting temperature of domain s3, presence of EDTA	Hathewaya histolytica
94.1	-	melting temperature of domain s3, presence of Ca2+	Hathewaya histolytica

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Release 2023.1 (January 2023)