Crystal Structure of a Putative Modulator of Gyrase (TldE) from Thermococcus kodakarensis

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Bibliographische Detailangaben
Zeitschriftentitel:	Crystals
Personen und Körperschaften:	Zhang, Xin, Li, Zhengqun, Zhao, Yanxiang, Cheng, Xilan, Liu, Yang, Zhang, Shihong, Liu, Junfeng
In:	Crystals, 9, 2019, 2, S. 107
Format:	E-Article
Sprache:	Englisch
veröffentlicht:	MDPI AG
Schlagwörter:	Inorganic Chemistry Condensed Matter Physics General Materials Science General Chemical Engineering

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Zusammenfassung:	<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>
Umfang:	107
ISSN:	2073-4352
DOI:	10.3390/cryst9020107