dc.contributor.author | Zhang, J | |
dc.contributor.author | Fan, F | |
dc.contributor.author | Zhao, Y | |
dc.contributor.author | Sun, L | |
dc.contributor.author | Liu, Y | |
dc.contributor.author | Keegan, RM | |
dc.contributor.author | Isupov, MN | |
dc.contributor.author | Wu, Y | |
dc.date.accessioned | 2018-07-18T14:14:49Z | |
dc.date.issued | 2017-02-28 | |
dc.description.abstract | Helicobacter pylori, a Gram-negative bacterial pathogen prevalent in the human population, is the causative agent of severe gastric diseases. An H. pylori type IV secretion (T4S) system encoded by the cytotoxin-associated gene pathogenicity island (cagPAI) is responsible for communication with host cells. As a component of the cagPAI T4S system core complex, CagX plays an important role in virulence-protein translocation into the host cells. In this work, the crystal structure of the C-terminal domain of CagX (CagXct), which is a homologue of the VirB9 protein from the VirB/D4 T4S system, is presented. CagXct is only the second three-dimensional structure to be elucidated of a VirB9-like protein. Another homologue, TraO, which is encoded on the Escherichia coli conjugative plasmid pKM101, shares only 19% sequence identity with CagXct; however, there is a remarkable similarity in tertiary structure between these two β-sandwich protein domains. Most of the residues that are conserved between CagXct and TraO are located within the protein core and appear to be responsible for the preservation of this domain fold. The studies presented here will contribute to our understanding of different bacterial T4S systems. | en_GB |
dc.description.sponsorship | The authors thank the staff of beamline BL17U1 at Shanghai
Synchrotron Radiation Facility (SSRF) for support during
diffraction data collection. We thank the National Natural
Science Foundation of China (Grant Nos. 31470741 and
31270790) and the National Thousand Talents Program of
China for their support of this work. | en_GB |
dc.identifier.citation | Vol. F73, pp. 167 - 173 | en_GB |
dc.identifier.doi | 10.1107/S2053230X17001376 | |
dc.identifier.uri | http://hdl.handle.net/10871/33486 | |
dc.language.iso | en | en_GB |
dc.publisher | International Union of Crystallography | en_GB |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pubmed/28291753 | en_GB |
dc.rights | This open-access article is distributed under the terms of the Creative Commons Attribution Licence
http://creativecommons.org/licenses/by/2.0/uk/legalcode, which permits unrestricted use, distribution, and
reproduction in any medium, provided the original authors and source are cited. | en_GB |
dc.subject | CagX | en_GB |
dc.subject | Helicobacter pylori | en_GB |
dc.subject | X-ray diffraction | en_GB |
dc.subject | cagPAI | en_GB |
dc.subject | crystal structure | en_GB |
dc.subject | cytotoxin-associated gene pathogenicity island | en_GB |
dc.subject | type IV secretion system | en_GB |
dc.subject | Amino Acid Sequence | en_GB |
dc.subject | Bacterial Proteins | en_GB |
dc.subject | Binding Sites | en_GB |
dc.subject | Cloning, Molecular | en_GB |
dc.subject | Crystallography, X-Ray | en_GB |
dc.subject | Escherichia coli | en_GB |
dc.subject | Escherichia coli Proteins | en_GB |
dc.subject | Gene Expression | en_GB |
dc.subject | Genomic Islands | en_GB |
dc.subject | Helicobacter pylori | en_GB |
dc.subject | Models, Molecular | en_GB |
dc.subject | Plasmids | en_GB |
dc.subject | Protein Binding | en_GB |
dc.subject | Protein Conformation, beta-Strand | en_GB |
dc.subject | Protein Folding | en_GB |
dc.subject | Protein Interaction Domains and Motifs | en_GB |
dc.subject | Protein Structure, Tertiary | en_GB |
dc.subject | Recombinant Proteins | en_GB |
dc.subject | Sequence Alignment | en_GB |
dc.subject | Structural Homology, Protein | en_GB |
dc.subject | Type IV Secretion Systems | en_GB |
dc.subject | Virulence Factors | en_GB |
dc.title | Crystal structure of the type IV secretion system component CagX from Helicobacter pylori. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2018-07-18T14:14:49Z | |
dc.identifier.issn | 2053-230X | |
exeter.place-of-publication | United States | en_GB |
dc.description | This is the final version. | en_GB |
dc.description | Available from the International Union of Crystallography via the DOI in this record. | en_GB |
dc.identifier.journal | Acta Crystallographica Section F: Structural Biology Communications | en_GB |