Chemical shift assignments for F-plasmid TraI (381-569).
Chemical shift assignments for F-plasmid TraI (381-569).
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DOI:
10.1007/s12104-010-9269-y
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发表时间:
2011-04
影响因子:
0.9
通讯作者:
Schildbach JF
中科院分区:
文献类型:
--
作者:
Wright NT;Majumdar A;Schildbach JF
TraI, the F plasmid-encoded nickase, is a 1,756 amino acid protein essential for conjugative transfer of F plasmid DNA from one bacterium to another. While crystal structures of N- and C-terminal domains of F TraI have been determined, central domains of the protein are structurally unexplored. These middle domains (between residues 306 and 1,500) are known to both bind single-stranded DNA (ssDNA) and unwind DNA through a highly processive helicase activity. Of this central region, the more C-terminal portion (~900–1500) appears related to helicase RecD of the E. coli RecBCD complex. The more N-terminal portion (306–900), however, shows limited sequence similarity to other proteins. In an attempt to define the structure of well-folded domains of this middle region and discern their function, we have isolated stable regions of TraI following limited proteolysis. One of these regions, TraI (381–569), was identified and a genetic construct encoding it was engineered. The protein was expressed, purified, and the sequence-specific chemical shifts for it were assigned.
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影响因子:
5.6
作者:
LLOSA, M;GRANDOSO, G;DELACRUZ, F
通讯作者:
DELACRUZ, F
影响因子:
5.6
作者:
Guogas, Laura M.;Kennedy, Sarah A.;Lee, Jin-Hyup;Redinbo, Matthew R.
通讯作者:
Redinbo, Matthew R.
DOI:
10.1073/pnas.90.7.2925
发表时间:
1993-04-01
影响因子:
11.1
作者:
PANSEGRAU, W;SCHRODER, W;LANKA, E
通讯作者:
LANKA, E
影响因子:
3.2
作者:
Dostal, Lubomir;Schildbach, Joel F.
通讯作者:
Schildbach, Joel F.
影响因子:
5.6
作者:
Llosa, M;Grandoso, G;delaCruz, F
通讯作者:
delaCruz, F