Literature summary for 3.4.21.110 extracted from

Kagawa, T.F.; OConnell, M.R.; Mouat, P.; Paoli, M.; OToole, P.W.; Cooney, J.C.
Model for substrate interactions in C5a peptidase from Streptococcus pyogenes: A 1.9 A crystal structure of the active form of ScpA (2009), J. Mol. Biol., 386, 754-772.

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Cloned(Commentary)

Cloned (Comment)	Organism
amino acid residues 31-1032 of the C5a peptidase gene are fused to GST and expressed in Escherichia coli. In addition expression as an N-terminal His-tagged C5a fusion protein in Escherichia coli	Streptococcus pyogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of an active form of ScpA is solved to 1.9 A resolution. The ScpA structure reveals that access to the catalytic site is restricted by variable regions in the catalytic domain and by the presence of the inserted protease-associated domain and the second fibronectin type III domains (Fn2). Modeling of the ScpA-C5a complex indicates that the substrate binds with carboxyl-terminal residues (65-74) extended through the active site and core residues (1-64) forming exosite-type interactions with the Fn2 domain. Substrate binding is anticipated to be dominated by ionic interactions in two distinct regions of ScpA. On the prime side of the active site, salt bridges are predicted between P1', P2', and P7' residues, and residues in the catalytic and PA domains. Remote to the active site, a larger number of ionic interactions between residues in the C5a core and the Fn2 domain are observed in the model. Thus, both PA and Fn2 domains are expected to play significant roles in substrate recognition	Streptococcus pyogenes

Crystallization (Comment)

Organism

crystal structure of an active form of ScpA is solved to 1.9 A resolution. The ScpA structure reveals that access to the catalytic site is restricted by variable regions in the catalytic domain and by the presence of the inserted protease-associated domain and the second fibronectin type III domains (Fn2). Modeling of the ScpA-C5a complex indicates that the substrate binds with carboxyl-terminal residues (65-74) extended through the active site and core residues (1-64) forming exosite-type interactions with the Fn2 domain. Substrate binding is anticipated to be dominated by ionic interactions in two distinct regions of ScpA. On the prime side of the active site, salt bridges are predicted between P1', P2', and P7' residues, and residues in the catalytic and PA domains. Remote to the active site, a larger number of ionic interactions between residues in the C5a core and the Fn2 domain are observed in the model. Thus, both PA and Fn2 domains are expected to play significant roles in substrate recognition

Streptococcus pyogenes

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pyogenes	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-terminal His-tagged C5a fusion protein + H2O	Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of cleaved HT-C5a indicate a loss of 830 Da, consistent with the removal of seven residues from the C-terminus	Streptococcus pyogenes	?	-	?

Synonyms

Synonyms	Comment	Organism
C5a peptidase	-	Streptococcus pyogenes
SCPA	-	Streptococcus pyogenes

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
20	-	assay at	Streptococcus pyogenes

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Streptococcus pyogenes