4JDO

Secreted chlamydial protein pgp3, coiled-coil deletion

Summary for 4JDO

• Entry DOI: 10.2210/pdb4jdo/pdb
• Related: 4JDM 4JDN
• Descriptor: Virulence plasmid protein pGP3-D, SODIUM ION (3 entities in total)
• Functional Keywords: virulence factor, secreted protein, chlamydia, inflammatory response, tnf, cell invasion
• Biological source: Chlamydia trachomatis
• Total number of polymer chains: 9
• Total formula weight: 208827.89

Authors

Galaleldeen, A.,Taylor, A.B.,Chen, D.,Holloway, S.P.,Zhong, G.,Hart, P.J. (deposition date: 2013-02-25, release date: 2013-06-05, Last modification date: 2023-12-06)

Primary citation

Galaleldeen, A.,Taylor, A.B.,Chen, D.,Schuermann, J.P.,Holloway, S.P.,Hou, S.,Gong, S.,Zhong, G.,Hart, P.J.
Structure of the Chlamydia trachomatis immunodominant antigen Pgp3.
J.Biol.Chem., 288:22068-22079, 2013

PubMed Abstract: Chlamydia trachomatis infection is the most common sexually transmitted bacterial disease. Left untreated, it can lead to ectopic pregnancy, pelvic inflammatory disease, and infertility. Here we present the structure of the secreted C. trachomatis protein Pgp3, an immunodominant antigen and putative virulence factor. The ∼84-kDa Pgp3 homotrimer, encoded on a cryptic plasmid, consists of globular N- and C-terminal assemblies connected by a triple-helical coiled-coil. The C-terminal domains possess folds similar to members of the TNF family of cytokines. The closest Pgp3 C-terminal domain structural homologs include a lectin from Burkholderia cenocepacia, the C1q component of complement, and a portion of the Bacillus anthracis spore surface protein BclA, all of which play roles in bioadhesion. The N-terminal domain consists of a concatenation of structural motifs typically found in trimeric viral proteins. The central parallel triple-helical coiled-coil contains an unusual alternating pattern of apolar and polar residue pairs that generate a rare right-handed superhelical twist. The unique architecture of Pgp3 provides the basis for understanding its role in chlamydial pathogenesis and serves as the platform for its optimization as a potential vaccine antigen candidate.

PubMed: 23703617
DOI: 10.1074/jbc.M113.475012

Experimental method

X-RAY DIFFRACTION (2.3 Å)