Crystal Structure of Borrelia turicatae protein, BTA121, a differentially regulated gene in the tick-mammalian transmission cycle of relapsing fever spirochetes.
Crystal Structure of Borrelia turicatae protein, BTA121, a differentially regulated gene in the tick-mammalian transmission cycle of relapsing fever spirochetes.
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DOI:
10.1038/s41598-017-14959-9
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发表时间:
2017-11-10
影响因子:
4.6
通讯作者:
Asojo OA
中科院分区:
文献类型:
--
作者:
Luo Z;Kelleher AJ;Darwiche R;Hudspeth EM;Shittu OK;Krishnavajhala A;Schneiter R;Lopez JE;Asojo OA
Tick-borne relapsing fever (RF) borreliosis is a neglected disease that is often misdiagnosed. RF species circulating in the United States include Borrelia turicatae, which is transmitted by argasid ticks. Environmental adaptation by RF Borrelia is poorly understood, however our previous studies indicated differential regulation of B. turicatae genes localized on the 150 kb linear megaplasmid during the tick-mammalian transmission cycle, including bta121. This gene is up-regulated by B. turicatae in the tick versus the mammal, and the encoded protein (BTA121) is predicted to be surface localized. The structure of BTA121 was solved by single-wavelength anomalous dispersion (SAD) using selenomethionine-derivative protein. The topology of BTA121 is unique with four helical domains organized into two helical bundles. Due to the sequence similarity of several genes on the megaplasmid, BTA121 can serve as a model for their tertiary structures. BTA121 has large interconnected tunnels and cavities that can accommodate ligands, notably long parallel helices, which have a large hydrophobic central pocket. Preliminary in-vitro studies suggest that BTA121 binds lipids, notably palmitate with a similar order of binding affinity as tablysin-15, a known palmitate-binding protein. The reported data will guide mechanistic studies to determine the role of BTA121 in the tick-mammalian transmission cycle of B. turicatae.
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影响因子:
5.8
作者:
Kozlikova, Barbora;Sebestova, Eva;Sochor, Jiri
通讯作者:
Sochor, Jiri
DOI:
10.1107/s0907444909052925
发表时间:
2010-02
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者:
Zwart PH
影响因子:
5.7
作者:
Kazimírová M;Štibrániová I
通讯作者:
Štibrániová I
DOI:
10.1107/s0907444904026460
发表时间:
2004-12-01
影响因子:
2.2
作者:
Krissinel, E;Henrick, K
通讯作者:
Henrick, K
影响因子:
4.3
作者:
Chovancova E;Pavelka A;Benes P;Strnad O;Brezovsky J;Kozlikova B;Gora A;Sustr V;Klvana M;Medek P;Biedermannova L;Sochor J;Damborsky J
通讯作者:
Damborsky J