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-Structure paper
Title | Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C. |
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Journal, issue, pages | Sci Rep, Vol. 7, Issue 1, Page 13018, Year 2017 |
Publish date | Oct 12, 2017 |
Authors | Shingo Nojima / Ayumi Fujishima / Koji Kato / Kayoko Ohuchi / Nobutaka Shimizu / Kento Yonezawa / Kenji Tajima / Min Yao / |
PubMed Abstract | Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit ...Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a β-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra α-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted α-helix. Such structural feature indicates that the inserted α-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the α-helical hinge may play important role for exporting glucan chains. |
External links | Sci Rep / PubMed:29026093 / PubMed Central |
Methods | SAS (X-ray synchrotron) / X-ray diffraction |
Resolution | 3.272 Å |
Structure data | SASDD53: PDB-5xw7: |
Source |
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Keywords | BIOSYNTHETIC PROTEIN / cellulose synthase / tetratrico peptide repeat |