spacer
View the latest EBI news stories and important announcements...
more

spacer
Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1dki

E.C. namestreptopain
SpeciesStreptococcus pyogenes (Bacteria)
E.C. Number (IntEnz) 3.4.22.10
CSA Homologues of 1dki1pvj,2jtc,2uzj,
CSA Entries With UniProtID P0C0J0
CSA Entries With EC Number 3.4.22.10
PDBe Entry 1dki
PDBSum Entry 1dki
MACiE Entry 1dki

Literature Report

IntroductionCysteine protease which is a virulance factor for many infectious diseases. It displays structural homology with papains despite having such low sequence identity with the superfamily that it merits being placed in a completely separate class.
MechansimCys 47 acts as the nucleophile for initial attack on the peptide substrate. The tetrahedral intermediate then collapses on protonation of the leaving group by His 195. This leaves an acyl-enzyme intermediate which is hydrolysed by an activated water molecule to complete the reaction.
Reaction

Catalytic Sites for 1dki

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerA47192macie:sideChainCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
SerA47192macie:mainChainAmideCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
HisA195340macie:sideChainProtonates leaving group to facilitate collapse of tetrahedral intermediate, then activates water to allow hydrolysis of acyl enzyme intermediate.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerB47192macie:sideChainCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
SerB47192macie:mainChainAmideCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
HisB195340macie:sideChainProtonates leaving group to facilitate collapse of tetrahedral intermediate, then activates water to allow hydrolysis of acyl enzyme intermediate.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerC47192macie:sideChainCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
SerC47192macie:mainChainAmideCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
HisC195340macie:sideChainProtonates leaving group to facilitate collapse of tetrahedral intermediate, then activates water to allow hydrolysis of acyl enzyme intermediate.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerD47192macie:sideChainCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
SerD47192macie:mainChainAmideCys 47 (appears as Ser 47 in pdb file) acts as nucleophile for initial attack on the peptide substrate to form an acyl enzyme intermediate. Also stabilises the tetrahedral intermediate via oxyanion hole.
HisD195340macie:sideChainProtonates leaving group to facilitate collapse of tetrahedral intermediate, then activates water to allow hydrolysis of acyl enzyme intermediate.

Literature References

Notes:
Gubba S
Replacement of histidine 340 with alanine inactivates the group A Streptococcus extracellular cysteine protease virulence factor.
Infect Immun 2000 68 3716-3719
PubMed: 10816533
Kagawa TF
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease.
Proc Natl Acad Sci U S A 2000 97 2235-2240
PubMed: 10681429
spacer
spacer