Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.

AUTOR(ES)

Holmgren, A

RESUMO

Detailed structural analyses revealed a family of periplasmic chaperones in Gram-negative prokaryotes which are structurally and possibly evolutionarily related to the immunoglobulin superfamily and assist in the assembly of adhesive pili. The members of this family have similar structures consistent with the overall topology of an immunoglobulin fold. Seven pilus chaperone sequences from Escherichia coli, Haemophilus influenzae and Klebsiella pneumoniae were aligned and their consensus sequence was superimposed onto the known three-dimensional structure of PapD, a representative member of the family. The molecular details of the conserved and variable structural motifs in this family of periplasmic chaperones give important insight into their structure, function, mechanism of action and evolutionary relationship with the immunoglobulin superfamily.

Documentos Relacionados

• Molecular basis of two subfamilies of immunoglobulin-like chaperones.
• Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits.
• Epigenetic regulation of killer immunoglobulin–like receptor expression in T cells
• New Immunoglobulin-like Molecules in the Serum of Bursectomized-Irradiated Chickens
• Activation of human eosinophils through leukocyte immunoglobulin-like receptor 7