4yvm

Publication Abstract from PubMed

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 (CagL(K74)) 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 CagL(K74). The structure displayed a six-helix bundle including two short alpha-helices, and the RGD motif was found in the long rigid alpha2 helix flanked by the conserved protease-sensitive and RGD-helper sequences, as observed in CagL(26695). However, two additional salt bridges were found between the helices compared with the CagL(26695) structure, suggesting that the putative flexible region harboring the RGD motif may be more stable in this CagL variant.

Crystal structure of CagL from Helicobacter pylori K74 strain.,Choi JM, Choi YH, Sudhanva MS, Devakumar S, Lee KH, Cha JH, Lee SH Biochem Biophys Res Commun. 2015 May 15;460(4):964-70. doi:, 10.1016/j.bbrc.2015.03.135. Epub 2015 Apr 1. PMID:25839651^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.