Crystal structure of CagL from Helicobacter pylori K74 strain

Jin Myung Choi, Yun Hui Choi, Muddenahalli Srinivasa Sudhanva, Sundaravinayagam Devakumar, Kun Ho Lee, Jeong Heon Cha, Sung Haeng Lee

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Abstract

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.

Original languageEnglish
Pages (from-to)964-970
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume460
Issue number4
DOIs
Publication statusPublished - 2015 May 12

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Choi, J. M., Choi, Y. H., Sudhanva, M. S., Devakumar, S., Lee, K. H., Cha, J. H., & Lee, S. H. (2015). Crystal structure of CagL from Helicobacter pylori K74 strain. Biochemical and Biophysical Research Communications, 460(4), 964-970. https://doi.org/10.1016/j.bbrc.2015.03.135