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Catalytic Site Atlas

CSA LITERATURE entry for 1oba

E.C. namelysozyme
SpeciesBacteriophage cp-1 ()
E.C. Number (IntEnz) 3.2.1.17
CSA Homologues of 1oba1h09,2ixu,2ixv,2j8f,2j8g,
CSA Entries With UniProtID P15057
CSA Entries With EC Number 3.2.1.17
PDBe Entry 1oba
PDBSum Entry 1oba
MACiE Entry 1oba

Literature Report

IntroductionCpl-1 lysin from Bacteriophage cp-1 catalyses the hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryote cell walls. On binding to choline, the enzymes geometry changes, its specificity increases, and catalytic activity is increased. Cpl-1 is used against bacteria such as Streptococcus pneumoniae (which causes pneumonia), as it kills the bacteria by breaking down its cell wall.
Mechansim1. Asp 10 acts as a general base, activating a water molecule for nucleophilic attack at the carbon atom of the glycosidic bond. 2. As the glycosidic bond cleaves, protonated Glu 94 acts as a general acid by protonating the leaving group oxygen atom.

Catalytic Sites for 1oba

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA1010macie:sideChainAsp 10 acts as a general base by deprotonating a water molecule, activating it for nucleophilic attack on the carbon atom of the glycosidic bond.
AspA182182macie:sideChainLow barrier hydrogen bonds allow the free transfer of protons between Asp 182 and Asp 10, ensuring the regeneration of the deprotonated state of Asp 10.
AspA9292macie:sideChainAsp 92 allows protons to move freely between itself and Glu 94, thus ensuring regeneration of the protonated state of Glu 94.
GluA9494macie:sideChainThe protonated form of Glu 94 acts as a general acid, by protonating the leaving group oxygen atom as the glycosidic bond is broken.

Literature References

Notes:
Hermoso JA
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Structure 2003 11 1239-1249
PubMed: 14527392
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