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TitleA Triple Mutant in the Omega-loop of TEM-1 beta-Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 290, Page 10382-10394, Year 2015
Publish dateNov 25, 2014 (structure data deposition date)
AuthorsStojanoski, V. / Chow, D.C. / Hu, L. / Sankaran, B. / Gilbert, H.F. / Prasad, B.V. / Palzkill, T.
External linksJ. Biol. Chem. / PubMed:25713062
MethodsX-ray diffraction
Resolution1.39 - 2.315 Å
Structure data

PDB-4rva:
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for deacylation
Method: X-RAY DIFFRACTION / Resolution: 1.4397 Å

PDB-4rx2:
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis
Method: X-RAY DIFFRACTION / Resolution: 2.315 Å

PDB-4rx3:
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

Chemicals

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-FLC:
CITRATE ANION

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / globular / beta-lactamase

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