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Abstract
The prokaryotic obligate intracellular pathogen Chlamydia trachomatis is the most prevalent cause of preventable blindness, affecting approximately six million people worldwide. In addition, C. trachomatis is the most commonly reported sexually transmitted pathogen in Europe and the US, causing pelvic inflammation, ectopic pregnancy and infertility. As in other intracellular pathogens, proteases play crucial roles during most stages of the complex life cycle of Chlamydia. CT441 is a chlamydial protease that has been reported to interfere with oestrogen signalling of the host cell. Here, the recombinant production, purification and crystallization of an inactive variant of CT441, designated CT441° (active-site Ser455 replaced by Ala), are described. CT441° was crystallized in space group P22121, with unit-cell parameters a = 86.7, b = 184.0, c = 209.6Å. A complete diffraction data set was collected to a resolution of 2.95Å.
Original language | English |
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Journal | Acta Crystallographica Section:F Structural Biology Communications |
Volume | 71 |
Pages (from-to) | 1454-1458 |
Number of pages | 5 |
DOIs | |
Publication status | Published - 01.01.2015 |
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
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Dive into the research topics of 'Production, crystallization and X-ray diffraction analysis of the protease CT441 from Chlamydia trachomatis'. Together they form a unique fingerprint.Projects
- 1 Finished
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The tail-specific protease (Tsp) of Chlamydiae spp.: Mechanistic and structural characterization of its interactions with host-cell proteins
01.02.14 → 31.01.18
Project: DFG Projects › DFG Individual Projects