4YVM

X-ray structure of Helicobacter pylori CagL-K74

Summary for 4YVM

• Entry DOI: 10.2210/pdb4yvm/pdb
• Descriptor: Cag pathogenicity island protein (2 entities in total)
• Functional Keywords: helicobacter pylori, t4ss, cagl, rgd domain, protein binding
• Biological source: Helicobacter pylori
• Total number of polymer chains: 2
• Total formula weight: 50063.51

Authors

Choi, J.M.,Choi, Y.H.,Cha, J.H.,Lee, S.H. (deposition date: 2015-03-20, release date: 2015-05-13, Last modification date: 2024-11-13)

Primary citation

Choi, J.M.,Choi, Y.H.,Sudhanva, M.S.,Devakumar, S.,Lee, K.H.,Cha, J.H.,Lee, S.H.
Crystal structure of CagL from Helicobacter pylori K74 strain.
Biochem.Biophys.Res.Commun., 460:964-970, 2015

PubMed 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 (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 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 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.

PubMed: 25839651
DOI: 10.1016/j.bbrc.2015.03.135

Experimental method

X-RAY DIFFRACTION (2.791 Å)