4.0 Article

Sequential backbone resonance assignments of the E-coli dihydrofolate reductase Gly67Val mutant: folate complex

期刊

BIOMOLECULAR NMR ASSIGNMENTS
卷 10, 期 1, 页码 125-129

出版社

SPRINGER
DOI: 10.1007/s12104-015-9650-y

关键词

E. coli dihydrofolate reductase; Folate complex; Gly67Val loop mutation; N-H/H-N and C-alpha/C-beta chemical shift assignments; Mutation-induced chemical shifts

资金

  1. Academic Frontier Program of the Ministry of Education, Culture, Sports, Science and Technology of Japan [07F010]
  2. Grants-in-Aid for Scientific Research [26291015, 26650023] Funding Source: KAKEN

向作者/读者索取更多资源

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 H-N, N-H, C-alpha and C-beta atoms of the Gly67Val mutant of E. coli DHFR complexed with folate at pH 7.0, 35 A degrees C, and then evaluated the H-N, N-H, C-alpha and C-beta 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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