2018
DOI: 10.1107/s2052252518007637
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Chlamydia protein Pgp3 studied at high resolution in a new crystal form

Abstract: Pgp3, a protein implicated in the sexually transmitted disease chlamydia, is described in a new crystal structure. It comprises a three-domain multi-macromolecular complex with two misaligned threefold axes; this comprised a unique challenge that has not been encountered before. 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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Cited by 5 publications
(10 citation statements)
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“…Across the present dataset, seven of the nine previously identified LGV-specific changes are maintained, but two amino acid replacements (T39K and D86N) also occur in many ocular and urogenital trachoma strains so are unlikely to contribute to LGV tropism. The two amino acids marked as being functionally significant in receptor binding (phenylalanine at amino acid site 6, and tryptophan at site 234) [22] are conserved across all sequences in the present dataset; however, a complete understanding of how the Pgp3 structure affects its biological function remains to be determined.…”
Section: Number Of 22 Bp Repeatsmentioning
confidence: 92%
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“…Across the present dataset, seven of the nine previously identified LGV-specific changes are maintained, but two amino acid replacements (T39K and D86N) also occur in many ocular and urogenital trachoma strains so are unlikely to contribute to LGV tropism. The two amino acids marked as being functionally significant in receptor binding (phenylalanine at amino acid site 6, and tryptophan at site 234) [22] are conserved across all sequences in the present dataset; however, a complete understanding of how the Pgp3 structure affects its biological function remains to be determined.…”
Section: Number Of 22 Bp Repeatsmentioning
confidence: 92%
“…This interaction of Pgp3 with host cell signalling pathways suggests that CDS5 may be subject to immune selection, and the accumulation of LGV-specific nonsynonymous SNPs in this gene may suggest a role in LGV tropism, a notion supported by the five-fold higher expression of Pgp-3 in LGV compared to ocular strains [8]. Additionally, the crystal structures of Pgp3 from a urogenital (serovar D) and LGV (L1 440) strain have been resolved [21,22]. Pgp3 differs in structure between the biovars, with nine amino acid changes being identified between the two strains, resulting in the LGV version of Pgp3 occupying a different space group to that of the serovar D Pgp3 protein [22].…”
Section: Number Of 22 Bp Repeatsmentioning
confidence: 97%
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