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-Structure paper
Title | Rearrangements of alpha-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export |
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Journal, issue, pages | Mol. Microbiol., Vol. 101, Page 656-670, Year 2016 |
Publish date | Feb 15, 2016 (structure data deposition date) |
Authors | Kinoshita, M. / Nakanishi, Y. / Furukawa, Y. / Namba, K. / Imada, K. / Minamino, T. |
External links | Mol. Microbiol. / PubMed:27178222 |
Methods | X-ray diffraction |
Resolution | 2.3 Å |
Structure data | PDB-5b3d: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | PROTEIN TRANSPORT / flagellar type III secretion / export chaperone / four-stranded coiled coil |