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