journal menu
![[Figure 1]](jb5065fig1mag.jpg)
|
|
Figure 1
PR10-10 cysteine-mutant crystal structures. (a) Disulfide-mediated linkage of PR10-10 homodimers. The conserved PR10-10 homodimer is indicated with protomers shown in green and cyan, and the β1 strands forming the center of the dimer interface are labeled. Conserved cysteines 21, 59 and 155 are shown in yellow and the disulfide-forming residues are shown in bold. Additionally, the continuation of the in-crystal polymer is designated. (b) PR10-10-Cys155Ser and PR10-10-Cys59Ser crystal structures determined in the absence of exogenous BIA ligands with bound unidentified ligands that were presumably copurified from E. coli, and the crystal structure of PR10-10-Cys59Ser with bound papaverine. Papaverine is shown in gray, whereas the unidentified ligands were not modeled. The key residues Cys59, Cys155, Ser59 and Ser155 and secondary-structural elements are labeled. The rainbow coloring scheme starts with the N-terminus in blue and ends with the C-terminus in red. |
![[Figure 1]](jb5065fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
