Skip to main content


Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Figure 1 | BMC Structural Biology

Figure 1

From: Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD

Figure 1

Dimer arrangement of the SycD:YopD complex. (A) Peptide-bound SycD forms a symmetric dimer, in which protomers are related by a crystallographic 2-fold axis. The dimerization is mediated via the two N-terminal helices (TPR1). (B) Dimerization interface of the SycD:YopD complex stabilized by van der Waal contacts involving the labeled residues shown as sticks. (C) Pairwise alignment (DaliLite server [29]) of SycD:YopD (green) to kinked apo SycD (red) (PDB ID: 2VGY) and to (D) monomer B of elongated apo SycD (orange) (PDB ID: 2VGX) shows that the dimer arrangement of the chaperone-peptide complex is nearly identical to the arrangement of the kinked apo form.

Back to article page