Abstract
Occasionally, a mutation in an exposed loop region causes a significant change in protein function and/or stability. A single mutation Gly67Val of E. coli dihydrofolate reductase (DHFR) in the exposed CD loop is such an example. We have carried out the chemical shift assignments for HN, NH, Cα and Cβ atoms of the Gly67Val mutant of E. coli DHFR complexed with folate at pH 7.0, 35 °C, and then evaluated the HN, NH, Cα and Cβ chemical shift changes caused by the mutation. The result indicates that, while the overall secondary structure remains the same, the single mutation Gly67Val causes site-specific conformational changes of the polypeptide backbone restricted around the adenosine-binding subdomain (residues 38–88) and not in the distant catalytic domain.
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This work was supported by the Academic Frontier Program 07F010 of the Ministry of Education, Culture, Sports, Science and Technology of Japan.
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Sunilkumar Puthenpurackal Narayanan and Akihiro Maeno have contributed equally to this work.
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Puthenpurackal Narayanan, S., Maeno, A., Wada, Y. et al. Sequential backbone resonance assignments of the E. coli dihydrofolate reductase Gly67Val mutant: folate complex. Biomol NMR Assign 10, 125–129 (2016). https://doi.org/10.1007/s12104-015-9650-y
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DOI: https://doi.org/10.1007/s12104-015-9650-y