Chlamydia protein Pgp3 studied at high resolution in a new crystal form

Sahir Khurshid, Lata Govada, Gillian Wills, Myra O. McClure, John R. Helliwell, Naomi E. Chayen
  • IUCrJ, June 2018, International Union of Crystallography
  • DOI: 10.1107/s2052252518007637

Structural analysis of Chlamydia protein Pgp3 by X-ray crystallography

What is it about?

The paper is about a challenging crystal structure analysis of the protein Pgp3 which is implicated in the sexually transmitted disease chlamydia. The X-ray crystal structure of Pgp3 from an LGV1 strain is reported at the highest X-ray diffraction resolution obtained to date for the full protein and compared with those of other crystal forms.

Why is it important?

The three-dimensional structure of this new crystal form is described, and the potassium bromide binding sites and the relevance to chlamydia isolates from around the globe are described. It is suggested that a specific intermolecular interaction, possibly of functional significance in receptor binding in chlamydia, might allow the design of a new chemotherapeutic agent against chlamydia.

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The following have contributed to this page: Professor John Richard Helliwell and Professor Naomi Esther Chayen