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Structure paper

TitleA low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the beta-lactamase BlaC.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 278, Page 134665-134665, Year 2024
Publish dateDec 13, 2023 (structure data deposition date)
AuthorsSun, J. / Boyle, A.L. / Brunle, S. / Ubbink, M.
External linksInt. J. Biol. Macromol. / PubMed:39134195
MethodsX-ray diffraction
Resolution1.42 - 2.3 Å
Structure data

PDB-8rfz:
Structure of E166A BlaC from Mycobacterium tuberculosis at pH 4.5
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-8rg2:
Structure of BlaC from Mycobacterium tuberculosis at pH 8
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-8rii:
Structure of E166A BlaC from Mycobacterium tuberculosis at pH 6.5
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / Beta-lactamase from Mycobacterium tuberculosis and encoded by blaC gene / free form Structure of BlaC from Mycobacterium tuberculosis at pH 8 / beta-lactamase

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