ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization and preliminary X-ray diffraction of the first periplasmic domain of SecDF, a translocon-associated membrane protein, from Thermus thermophilus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- 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
- Dynamic interaction of the sec translocon with the chaperone PpiD.The Journal of biological chemistry · 2014Article
- The mechanism of protein export enhancement by the SecDF membrane component.Biophysics (Nagoya-shi, Japan) · 2011Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A membrane-integrated Sec component, SecDF, associates with the SecYEG protein-conducting channel and facilitates protein secretion and membrane-protein integration. SecDF contains 12 transmembrane helices and two periplasmic domains. The first periplasmic domain (P1) plays an important role in protein translocation. Here, the overexpression, purification and crystallization of the P1 domain of Thermus thermophilus SecDF are reported. The crystals diffracted X-rays to 2.3 Å resolution and belonged to space group C2, with unit-cell parameters a = 161.1, b = 35.8, c = 181.6 Å, suggesting that they contain four molecules per asymmetric unit. The initial phases were determined by the multiple-wavelength anomalous dispersion method using selenomethionine-labelled crystals.
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