Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution

被引:8
作者
Barta, Michael L. [1 ]
Hickey, John [2 ]
Kemege, Kyle E. [1 ]
Lovell, Scott [3 ]
Battaile, Kevin P. [4 ]
Hefty, P. Scott [1 ]
机构
[1] Univ Kansas, Dept Mol Biosci, Lawrence, KS 66045 USA
[2] Univ Kansas, Dept Pharmaceut Chem, Lawrence, KS 66045 USA
[3] Univ Kansas, Prot Struct Lab, Del Shankel Struct Biol Ctr, Lawrence, KS 66047 USA
[4] Hauptman Woodward Med Res Inst, IMCA CAT, Argonne, IL 60439 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金
美国国家卫生研究院;
关键词
III SECRETION APPARATUS; SHIGELLA-FLEXNERI; SYSTEM NEEDLE; IPAD; TIP; RECRUITMENT; PHENIX;
D O I
10.1107/S1744309113027371
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Chlamydia trachomatis is a major cause of various diseases, including blinding trachoma and pelvic inflammatory disease, and is the leading reported sexually transmitted bacterial infection worldwide. All pathogenic Chlamydiae spp. utilize a supramolecular syringe, or type III secretion system (T3SS), to inject proteins into their obligate host in order to propagate infection. Here, the structure of CT584, a T3SS-associated protein, that has been refined to a resolution of 3.05 angstrom is reported. The CT584 structure is a hexamer comprised of a trimer of dimers. The structure shares a high degree of similarity to the recently reported structure of an orthologous protein, Cpn0803, from Chlamydia pneumoniae, which highlights the highly conserved nature of this protein across these chlamydial species, despite different tissue tropism and disease pathology.
引用
收藏
页码:1196 / 1201
页数:6
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