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Catalytic Site Atlas

CSA LITERATURE entry for 1oba

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

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