Disulfide-linked oligomers of the major outer membrane protein of chlamydiae.
The major outer membrane protein of chlamydial elementary bodies was identified in dimer, trimer, and other multimeric forms. These natural multimers were stabilized by disulfide-mediated cross-linking. Such cross-linking of outer membrane proteins may play an important role in the formation and evolution of chlamydial cell wall structure.
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002692:Chlamydia trachomatis / Q000032:analysis*; D002691:Chlamydophila psittaci / Q000032:analysis*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000032:analysis*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins