ArticleJournal of bacteriology2010
Structure and protein-protein interaction studies on Chlamydia trachomatis protein CT670 (YscO Homolog).
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- The Fish Pathogen "Candidatus Clavichlamydia salmonicola"-A Missing Link in the Evolution of Chlamydial Pathogens of Humans.Genome biology and evolution · 2023Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.Acta crystallographica. Section F, Structural biology communications · 2022Article
- "The structure of the Type III secretion system export gate with CdsO, an ATPase lever arm".PLoS pathogens · 2020Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
- Article
- Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromFrontiers in microbiology · 2018Article
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Building a secreting nanomachine: a structural overview of the T3SS.Current opinion in structural biology · 2014Review
- Functionally essential interaction between Yersinia YscO and the T3S4 domain of YscP.Journal of bacteriology · 2013Article
- Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus.PloS one · 2013Article
- Ab initio structural modeling of and experimental validation for Chlamydia trachomatis protein CT296 reveal structural similarity to Fe(II) 2-oxoglutarate-dependent enzymes.Journal of bacteriology · 2011Article
- Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.Nature structural & molecular biology · 2011Article
- The Chlamydial Type III Secretion Mechanism: Revealing Cracks in a Tough Nut.Frontiers in microbiology · 2010Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Comparative genomic studies have identified many proteins that are found only in various Chlamydiae species and exhibit no significant sequence similarity to any protein in organisms that do not belong to this group. The CT670 protein of Chlamydia trachomatis is one of the proteins whose genes are in one of the type III secretion gene clusters but whose cellular functions are not known. CT670 shares several characteristics with the YscO protein of Yersinia pestis, including the neighboring genes, size, charge, and secondary structure, but the structures and/or functions of these proteins remain to be determined. Although a BLAST search with CT670 did not identify YscO as a related protein, our analysis indicated that these two proteins exhibit significant sequence similarity. In this paper, we report that the CT670 crystal, solved at a resolution of 2 A, consists of a single coiled coil containing just two long helices. Gel filtration and analytical ultracentrifugation studies showed that in solution CT670 exists in both monomeric and dimeric forms and that the monomer predominates at lower protein concentrations. We examined the interaction of CT670 with many type III secretion system-related proteins (viz., CT091, CT665, CT666, CT667, CT668, CT669, CT671, CT672, and CT673) by performing bacterial two-hybrid assays. In these experiments, CT670 was found to interact only with the CT671 protein (YscP homolog), whose gene is immediately downstream of ct670. A specific interaction between CT670 and CT671 was also observed when affinity chromatography pull-down experiments were performed. These results suggest that CT670 and CT671 are putative homologs of the YcoO and YscP proteins, respectively, and that they likely form a chaperone-effector pair.
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