The N-terminal domain of MuB protein has striking structural similarity to DNA-binding domains and mediates MuB filament–filament interactions
M Dramićanin, B López-Méndez, J Boskovic… - Journal of structural …, 2015 - Elsevier
MuB is an ATP-dependent DNA-binding protein that regulates the activity of MuA
transposase and delivers the target DNA for transposition of phage Mu. Mechanistic insight
into MuB function is limited to its AAA+ ATPase module, which upon ATP binding assembles
into helical filaments around the DNA. However, the structure and function of the flexible N-
terminal domain (NTD) appended to the AAA+ module remains uncharacterized. Here we
report the solution structure of MuB NTD determined by NMR spectroscopy. The structure …
transposase and delivers the target DNA for transposition of phage Mu. Mechanistic insight
into MuB function is limited to its AAA+ ATPase module, which upon ATP binding assembles
into helical filaments around the DNA. However, the structure and function of the flexible N-
terminal domain (NTD) appended to the AAA+ module remains uncharacterized. Here we
report the solution structure of MuB NTD determined by NMR spectroscopy. The structure …
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