Structure and function of the dihydropteroate synthase from staphylococcus aureus 1 1Edited by R. Huber
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 268, Issue: 1, Page: 21-30
1997
- 159Citations
- 79Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations159
- Citation Indexes159
- 159
- CrossRef126
- Captures79
- Readers79
- 79
- Mentions1
- References1
- 1
Article Description
The gene encoding the dihydropteroate synthase of staphylococcus aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and X-ray crystallographic studies. The enzyme is a dimer in solution, has a steady state kinetic mechanism that suggests random binding of the two substrates and half-site reactivity. The crystal structure of apo-enzyme and a binary complex with the substrate analogue hydroxymethylpterin pyrophosphate were determined at 2.2 Å and 2.4 Å resolution, respectively. The enzyme belongs to the group of “ TIM-barrel” proteins and crystallizes as a non-crystallographic dimer. Only one molecule of the substrate analogue bound per dimer in the crystal. Sequencing of nine sulfonamide-resistant clinical isolates has shown that as many as 14 residues could be involved in resistance development. The residues are distributed over the surface of the protein, which defies a simple interpretation of their roles in resistance. Nevertheless, the three-dimensional structure of the substrate analogue binary complex could give important insight into the molecular mechanism of this enzyme.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002228369790944X; http://dx.doi.org/10.1006/jmbi.1997.0944; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031585986&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9149138; https://linkinghub.elsevier.com/retrieve/pii/S002228369790944X; https://dx.doi.org/10.1006/jmbi.1997.0944
Elsevier BV
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