Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5914158 | Journal of Structural Biology | 2014 | 13 Pages |
Abstract
Cyto-GspL interacts not only with the N1E domain, but also with the CTE domain and is even in contact with AMPPNP. Moreover, the cyto-GspL domains engage in two types of mutual interactions, resulting in two essentially identical, but crystallographically independent, “cyto-GspL rods” that run throughout the crystal. Very similar rods are present in previous crystals of cyto-GspL and of the N1E
- cyto-GspL complex. This arrangement, now seen four times in three entirely different crystal forms, involves contacts between highly conserved residues suggesting a role in the biogenesis or the secretion mechanism or both of the T2SS.
- cyto-GspL complex. This arrangement, now seen four times in three entirely different crystal forms, involves contacts between highly conserved residues suggesting a role in the biogenesis or the secretion mechanism or both of the T2SS.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Connie Lu, Konstantin V. Korotkov, Wim G.J. Hol,