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Structure paper

TitleThe hydrolytic water molecule of Class A beta-lactamase relies on the acyl-enzyme intermediate ES* for proper coordination and catalysis.
Journal, issue, pagesSci Rep, Vol. 10, Page 10205-10205, Year 2020
Publish dateMar 6, 2018 (structure data deposition date)
AuthorsHe, Y. / Lei, J. / Pan, X. / Huang, X. / Zhao, Y.
External linksSci Rep / PubMed:32576842
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-5zfl:
Crystal structure of beta-lactamase PenP mutant E166Y
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-5zft:
Crystal structure of beta-lactamase PenP mutant-E166Y in complex with cephaloridine as "pre-deacylation" intermediate
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-5zg6:
Crystal structure of beta-lactamase PenP mutant-E166Y in complex with cephaloridine as "post-acylation" intermediate
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-CED:
5-METHYL-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID

Source
  • bacillus licheniformis (bacteria)
KeywordsHYDROLASE / class A beta-lactamase / antibiotic resistance

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