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

The protein Pgp3 is implicated in the sexually transmitted disease chlamydia and comprises an extended complex arrangement of a C-terminal domain (CTD) and an N-terminal domain (NTD) linked by a triple-helix coiled coil (THCC). Here, the X-ray crystal structure of Pgp3 from an LGV1 strain is reporte...

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Autores principales: Khurshid, Sahir, Govada, Lata, Wills, Gillian, McClure, Myra O., Helliwell, John R., Chayen, Naomi E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6038952/
https://www.ncbi.nlm.nih.gov/pubmed/30002845
http://dx.doi.org/10.1107/S2052252518007637
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author Khurshid, Sahir
Govada, Lata
Wills, Gillian
McClure, Myra O.
Helliwell, John R.
Chayen, Naomi E.
author_facet Khurshid, Sahir
Govada, Lata
Wills, Gillian
McClure, Myra O.
Helliwell, John R.
Chayen, Naomi E.
author_sort Khurshid, Sahir
collection PubMed
description The protein Pgp3 is implicated in the sexually transmitted disease chlamydia and comprises an extended complex arrangement of a C-terminal domain (CTD) and an N-terminal domain (NTD) linked by a triple-helix coiled coil (THCC). Here, 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. The protein was crystallized using a high concentration of potassium bromide, which resulted in a new crystal form with relatively low solvent content that diffracted to a resolution of 1.98 Å. The three-dimensional structure of this new crystal form is described and compared with those of other crystal forms, and the potassium bromide binding sites and the relevance to chlamydia isolates from around the globe are described. The crystal packing is apparently driven by the CTDs. Since the threefold axes of the THCC and NTD are not collinear with the threefold axis of a CTD, this naturally leads to disorder in the THCC and the portion of the NTD that does not directly interact with the CTD via crystal packing. The key avenue to resolving these oddities in the crystal structure analysis was a complete new analysis in space group P1 and determining the space group as P2(1)2(1)2(1). This space-group assignment was that originally determined from the diffraction pattern but was perhaps complicated by translational noncrystallographic symmetry. This crystal structure of a three-domain multi-macromolecular complex with two misaligned threefold axes was a unique challenge and has not been encountered before. 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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spelling pubmed-60389522018-07-12 Chlamydia protein Pgp3 studied at high resolution in a new crystal form Khurshid, Sahir Govada, Lata Wills, Gillian McClure, Myra O. Helliwell, John R. Chayen, Naomi E. IUCrJ Research Papers The protein Pgp3 is implicated in the sexually transmitted disease chlamydia and comprises an extended complex arrangement of a C-terminal domain (CTD) and an N-terminal domain (NTD) linked by a triple-helix coiled coil (THCC). Here, 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. The protein was crystallized using a high concentration of potassium bromide, which resulted in a new crystal form with relatively low solvent content that diffracted to a resolution of 1.98 Å. The three-dimensional structure of this new crystal form is described and compared with those of other crystal forms, and the potassium bromide binding sites and the relevance to chlamydia isolates from around the globe are described. The crystal packing is apparently driven by the CTDs. Since the threefold axes of the THCC and NTD are not collinear with the threefold axis of a CTD, this naturally leads to disorder in the THCC and the portion of the NTD that does not directly interact with the CTD via crystal packing. The key avenue to resolving these oddities in the crystal structure analysis was a complete new analysis in space group P1 and determining the space group as P2(1)2(1)2(1). This space-group assignment was that originally determined from the diffraction pattern but was perhaps complicated by translational noncrystallographic symmetry. This crystal structure of a three-domain multi-macromolecular complex with two misaligned threefold axes was a unique challenge and has not been encountered before. 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. International Union of Crystallography 2018-06-07 /pmc/articles/PMC6038952/ /pubmed/30002845 http://dx.doi.org/10.1107/S2052252518007637 Text en © Khurshid et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/
spellingShingle Research Papers
Khurshid, Sahir
Govada, Lata
Wills, Gillian
McClure, Myra O.
Helliwell, John R.
Chayen, Naomi E.
Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title_full Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title_fullStr Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title_full_unstemmed Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title_short Chlamydia protein Pgp3 studied at high resolution in a new crystal form
title_sort chlamydia protein pgp3 studied at high resolution in a new crystal form
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6038952/
https://www.ncbi.nlm.nih.gov/pubmed/30002845
http://dx.doi.org/10.1107/S2052252518007637
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