Next Article in Journal
The Use of Size Exclusion Chromatography to Monitor Protein Self-Assembly
Previous Article in Journal
Formation of Metastable Crystals from Supercooled, Supersaturated, and Supercompressed Liquids: Role of Crystal-Liquid Interfacial Free Energy
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessCommunication
Crystals 2017, 7(11), 330; doi:10.3390/cryst7110330

Crystallisation and Preliminary Crystallographic Analysis of Helicobacter pylori Periplasmic Binding Protein YckK

Department of Microbiology, Monash University, Clayton, VIC 3800, Australia
Infection and Immunity Program, Monash Biomedicine Discovery Institute, Clayton, VIC 3800, Australia
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Albert Guskov
Received: 7 September 2017 / Revised: 26 October 2017 / Accepted: 26 October 2017 / Published: 29 October 2017
(This article belongs to the Section Biomolecular Crystals)
View Full-Text   |   Download PDF [2760 KB, uploaded 29 October 2017]   |  


Helicobacter pylori infection can lead to the development of gastric and duodenal ulcers and gastric cancer. In recent years, the efficacy of the standard therapy has been falling, necessitating ongoing efforts to identify new drug targets. Due to their important role in chemotaxis and nutrient uptake, periplasmic binding proteins (PBPs) represent potential targets for new antimicrobial agents that have not yet been fully explored and exploited. The H. pylori PBP YckK is homologous to polar amino acid-binding proteins from other bacteria. The yckK gene overlaps the gene tcyB—a gene annotated as a polar amino acid-transporting permease. Purified recombinant YckK behaved as a monomer in solution. Crystals of YckK were grown by the hanging drop vapour diffusion method using PEG 3350 as the precipitating agent. The crystals belong to the primitive triclinic space group P1 with unit cell parameters a = 63.0, b = 63.5, c = 74.6 Å, α = 72.5, β = 68.3, γ = 69.4°. X-ray diffraction data were collected to 1.8 Å resolution using synchrotron radiation. Molecular replacement using this data revealed that the asymmetric unit contains three subunits: two in the open and one in the closed conformation. View Full-Text
Keywords: Helicobacter pylori; periplasmic binding protein; protein crystallisation Helicobacter pylori; periplasmic binding protein; protein crystallisation

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Rahman, M.M.; Germantsis, D.P.; Machuca, M.A.; Ud-Din, A.I.S.; Roujeinikova, A. Crystallisation and Preliminary Crystallographic Analysis of Helicobacter pylori Periplasmic Binding Protein YckK. Crystals 2017, 7, 330.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Crystals EISSN 2073-4352 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top