ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Purification, crystallization and preliminary X-ray diffraction of SecDF, a translocon-associated membrane protein, from Thermus thermophilus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Crystal structure of a YeeE/YedE family protein engaged in thiosulfate uptake.Science advances · 2020Article
- Electric-Field-Induced Protein Translocation via a Conformational Transition in SecDF: An MD Study.Biophysical journal · 2017Article
- Conformational variation of the translocon enhancing chaperone SecDF.Journal of structural and functional genomics · 2014Article
- Membrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors.Journal of bacteriology · 2013Article
- Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data.International journal of molecular sciences · 2012Article
- Crystallization and preliminary X-ray diffraction of the first periplasmic domain of SecDF, a translocon-associated membrane protein, from Thermus thermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Article
- The mechanism of protein export enhancement by the SecDF membrane component.Biophysics (Nagoya-shi, Japan) · 2011Review
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermus thermophilus has a multi-path membrane protein, TSecDF, as a single-chain homologue of Escherichia coli SecD and SecF, which form a translocon-associated complex required for efficient preprotein translocation and membrane-protein integration. Here, the cloning, expression in E. coli, purification and crystallization of TSecDF are reported. Overproduced TSecDF was solubilized with dodecylmaltoside, chromatographically purified and crystallized by vapour diffusion in the presence of polyethylene glycol. The crystals yielded a maximum resolution of 4.2 angstroms upon X-ray irradiation, revealing that they belonged to space group P4(3)2(1)2. Attempts were made to improve the diffraction quality of the crystals by combinations of micro-stirring, laser-light irradiation and dehydration, which led to the eventual collection of complete data sets at 3.74 angstroms resolution and preliminary success in the single-wavelength anomalous dispersion analysis. These results provide information that is essential for the determination of the three-dimensional structure of this important membrane component of the protein-translocation machinery.
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