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Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis
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| Zeitschriftentitel: | Crystals |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | Crystals, 9, 2019, 2, S. 107 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
MDPI AG
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| Schlagwörter: |
| author_facet |
Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng |
|---|---|
| author |
Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng |
| spellingShingle |
Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng Crystals Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis Inorganic Chemistry Condensed Matter Physics General Materials Science General Chemical Engineering |
| author_sort |
zhang, xin |
| spelling |
Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng 2073-4352 MDPI AG Inorganic Chemistry Condensed Matter Physics General Materials Science General Chemical Engineering http://dx.doi.org/10.3390/cryst9020107 <jats:p>TldD and TldE proteins interact and form a complex to degrade unfolded peptides. The gene Tk0499 from Thermococcus kodakarensis encoded a putative modulator of gyrase (TkTldE). Although TldE genes were common in bacteria and archaea, the structural basis on the evolution of proteins remained largely unknown. Here, the three-dimensional structure of TkTldE was determined by X-ray diffraction. Crystals were acquired by the sitting-drop vapor-diffusion method. X-ray diffraction data from crystals were collected at 2.35 Å. The space group and unit-cell parameters suggested that there were two molecules in the asymmetric unit. Our results showed that TkTldE forms a homodimer, which contained anti-parallel β-strands and a pair of α-helices. Comparison of the structures of TldE and TldD showed that despite their high sequence similarity, TldE lacked the conserved HExxxH and GxC motif in which two His and a Cys residues bound a metal ion. Taken together, these results provided insight into the structural information of this class of TldE/TldD.</jats:p> Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis Crystals |
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| title |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_unstemmed |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_full |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_fullStr |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_full_unstemmed |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_short |
Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_sort |
crystal structure of a putative modulator of gyrase (tlde) from thermococcus kodakarensis |
| topic |
Inorganic Chemistry Condensed Matter Physics General Materials Science General Chemical Engineering |
| url |
http://dx.doi.org/10.3390/cryst9020107 |
| publishDate |
2019 |
| physical |
107 |
| description |
<jats:p>TldD and TldE proteins interact and form a complex to degrade unfolded peptides. The gene Tk0499 from Thermococcus kodakarensis encoded a putative modulator of gyrase (TkTldE). Although TldE genes were common in bacteria and archaea, the structural basis on the evolution of proteins remained largely unknown. Here, the three-dimensional structure of TkTldE was determined by X-ray diffraction. Crystals were acquired by the sitting-drop vapor-diffusion method. X-ray diffraction data from crystals were collected at 2.35 Å. The space group and unit-cell parameters suggested that there were two molecules in the asymmetric unit. Our results showed that TkTldE forms a homodimer, which contained anti-parallel β-strands and a pair of α-helices. Comparison of the structures of TldE and TldD showed that despite their high sequence similarity, TldE lacked the conserved HExxxH and GxC motif in which two His and a Cys residues bound a metal ion. Taken together, these results provided insight into the structural information of this class of TldE/TldD.</jats:p> |
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| author | Zhang, Xin, Li, Zhengqun, Zhao, Yanxiang, Cheng, Xilan, Liu, Yang, Zhang, Shihong, Liu, Junfeng |
| author_facet | Zhang, Xin, Li, Zhengqun, Zhao, Yanxiang, Cheng, Xilan, Liu, Yang, Zhang, Shihong, Liu, Junfeng, Zhang, Xin, Li, Zhengqun, Zhao, Yanxiang, Cheng, Xilan, Liu, Yang, Zhang, Shihong, Liu, Junfeng |
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| description | <jats:p>TldD and TldE proteins interact and form a complex to degrade unfolded peptides. The gene Tk0499 from Thermococcus kodakarensis encoded a putative modulator of gyrase (TkTldE). Although TldE genes were common in bacteria and archaea, the structural basis on the evolution of proteins remained largely unknown. Here, the three-dimensional structure of TkTldE was determined by X-ray diffraction. Crystals were acquired by the sitting-drop vapor-diffusion method. X-ray diffraction data from crystals were collected at 2.35 Å. The space group and unit-cell parameters suggested that there were two molecules in the asymmetric unit. Our results showed that TkTldE forms a homodimer, which contained anti-parallel β-strands and a pair of α-helices. Comparison of the structures of TldE and TldD showed that despite their high sequence similarity, TldE lacked the conserved HExxxH and GxC motif in which two His and a Cys residues bound a metal ion. Taken together, these results provided insight into the structural information of this class of TldE/TldD.</jats:p> |
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| physical | 107 |
| publishDate | 2019 |
| publishDateSort | 2019 |
| publisher | MDPI AG |
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| series | Crystals |
| source_id | 49 |
| spelling | Zhang, Xin Li, Zhengqun Zhao, Yanxiang Cheng, Xilan Liu, Yang Zhang, Shihong Liu, Junfeng 2073-4352 MDPI AG Inorganic Chemistry Condensed Matter Physics General Materials Science General Chemical Engineering http://dx.doi.org/10.3390/cryst9020107 <jats:p>TldD and TldE proteins interact and form a complex to degrade unfolded peptides. The gene Tk0499 from Thermococcus kodakarensis encoded a putative modulator of gyrase (TkTldE). Although TldE genes were common in bacteria and archaea, the structural basis on the evolution of proteins remained largely unknown. Here, the three-dimensional structure of TkTldE was determined by X-ray diffraction. Crystals were acquired by the sitting-drop vapor-diffusion method. X-ray diffraction data from crystals were collected at 2.35 Å. The space group and unit-cell parameters suggested that there were two molecules in the asymmetric unit. Our results showed that TkTldE forms a homodimer, which contained anti-parallel β-strands and a pair of α-helices. Comparison of the structures of TldE and TldD showed that despite their high sequence similarity, TldE lacked the conserved HExxxH and GxC motif in which two His and a Cys residues bound a metal ion. Taken together, these results provided insight into the structural information of this class of TldE/TldD.</jats:p> Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis Crystals |
| spellingShingle | Zhang, Xin, Li, Zhengqun, Zhao, Yanxiang, Cheng, Xilan, Liu, Yang, Zhang, Shihong, Liu, Junfeng, Crystals, Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis, Inorganic Chemistry, Condensed Matter Physics, General Materials Science, General Chemical Engineering |
| title | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_full | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_fullStr | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_full_unstemmed | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_short | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| title_sort | crystal structure of a putative modulator of gyrase (tlde) from thermococcus kodakarensis |
| title_unstemmed | Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis |
| topic | Inorganic Chemistry, Condensed Matter Physics, General Materials Science, General Chemical Engineering |
| url | http://dx.doi.org/10.3390/cryst9020107 |