A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.
A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.
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DOI:
10.1016/j.jmb.2008.12.057
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发表时间:
2009-02-20
影响因子:
5.6
通讯作者:
Redinbo, Matthew R.
中科院分区:
文献类型:
--
作者:
Guogas, Laura M.;Kennedy, Sarah A.;Lee, Jin-Hyup;Redinbo, Matthew R.
The TraI relaxase-helicase is the central catalytic component of the multi-protein relaxosome complex responsible for conjugative DNA transfer (CDT) between bacterial cells. CDT is a primary mechanism for the lateral propagation of microbial genetic material, including the spread of antibiotic resistance genes. The 2.4 Å resolution crystal structure of the C-terminal domain of the multifunctional Escherichia coli F plasmid TraI protein (TraI-CT) is presented, and specific structural regions essential for CDT are identified. The crystal structure reveals a novel fold composed of a 28-residue N-terminal α-Domain connected by a proline-rich loop to a compact α/β-Domain. Both the globular nature of the α/β-Domain and the presence and rigidity of the proline-rich loop are required for DNA transfer and single-stranded DNA binding. Taken together, these data establish the specific structural features of this non-catalytic domain that are essential to DNA conjugation.
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
3.2
作者:
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影响因子:
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Fekete, RA;Frost, LS
通讯作者:
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DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
DOI:
10.1107/s0907444997011980
发表时间:
1998-07-01
影响因子:
2.2
作者:
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通讯作者:
Main, P