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TitleMutations in PBP2 from ceftriaxone-resistant Neisseria gonorrhoeae alter the dynamics of the beta 3-beta 4 loop to favor a low-affinity drug-binding state.
Journal, issue, pagesJ. Biol. Chem., Vol. 297, Page 101188-101188, Year 2021
Publish dateJul 10, 2020 (structure data deposition date)
AuthorsFenton, B.A. / Tomberg, J. / Sciandra, C.A. / Nicholas, R.A. / Davies, C. / Zhou, P.
External linksJ. Biol. Chem. / PubMed:34529975
MethodsX-ray diffraction
Resolution1.9 - 2.15 Å
Structure data

PDB-6xqv:
Crystal structure of the catalytic domain of PBP2 S310A from Neisseria gonorrhoeae in a pre-acylation complex with ceftriaxone
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-6xqx:
Crystal structure of the catalytic domain of PBP2 S310A from Neisseria gonorrhoeae with the H514A mutation at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6xqy:
Crystal structure of the catalytic domain of PBP2 S310A from Neisseria gonorrhoeae at pH 9.5
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6xqz:
Crystal structure of the catalytic domain of PBP2 S310A from Neisseria gonorrhoeae at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

Chemicals

ChemComp-9F2:
Ceftriaxone / antibiotic*YM

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • neisseria gonorrhoeae (bacteria)
KeywordsHYDROLASE / PBP2 / beta-lactam / antibiotic target / ceftriaxone / TRANSFERASE

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