Helicobacter pylori (Hp) CagL is a component of the type IV secretion system (T4SS) and interacts with integrin in host cells through its flexible RGD domain to translocate CagA. Differences in CagL amino acid polymorphisms between Western and East-Asian Hps are correlated with clinical outcome. CagL of East-Asian clinical Hp isolate K74 (CagLK74) contains multiple residue variations upstream of RGD motif and has different integrin binding affinities compared to those of CagL from Western Hp 26695. Here, we report the crystal structure of CagLK74. The structure displayed a six-helix bundle including two short α-helices, and the RGD motif was found in the long rigid α2 helix flanked by the conserved protease-sensitive and RGD-helper sequences, as observed in CagL26695. However, two additional salt bridges were found between the helices compared with the CagL26695 structure, suggesting that the putative flexible region harboring the RGD motif may be more stable in this CagL variant.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2015 May 12|
Bibliographical notePublisher Copyright:
© 2015 Elsevier Inc. All rights reserved.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology