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TitleExploiting antigenic diversity for vaccine design: the Chlamydia ArtJ paradigm.
Journal, issue, pagesJ. Biol. Chem., Year 2010
Publish dateJun 10, 2008 (structure data deposition date)
AuthorsSoriani, M. / Petit, P. / Grifantini, R. / Petracca, R. / Gancitano, G. / Frigimelica, E. / Nardelli, F. / Garcia, C. / Spinelli, S. / Scarabelli, G. ...Soriani, M. / Petit, P. / Grifantini, R. / Petracca, R. / Gancitano, G. / Frigimelica, E. / Nardelli, F. / Garcia, C. / Spinelli, S. / Scarabelli, G. / Fiorucci, S. / Affentranger, R. / Ferrer-Navarro, M. / Zacharias, M. / Colombo, G. / Vuillard, L. / Daura, X. / Grandi, G.
External linksJ. Biol. Chem. / PubMed:20592031
MethodsX-ray diffraction
Resolution1.92 - 2.1 Å
Structure data

PDB-3del:
The structure of CT381, the arginine binding protein from the periplasm Chlamydia trachomatis
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-3n26:
Cpn0482 : the arginine binding protein from the periplasm of chlamydia Pneumoniae
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ARG:
ARGININE

Source
  • chlamydia trachomatis (bacteria)
  • chlamydophila pneumoniae (bacteria)
KeywordsPROTEIN BINDING / TRANSPORT PROTEIN / Alpha and Beta protein (a/b) / periplasmic protein / arginine binding / Vaccine development / Structural Genomics / BacAbs - EU FP6 programme / Marseilles Structural Genomics Program @ AFMB / MSGP

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