journal menu
![[Figure 1]](ji5016fig1mag.jpg)
|
|
Figure 1
Crystal structure of the VASH1c–SVBP complex. (a) The VASH1c–SVBP crystal structure in the asymmetric unit. VASH1c is colored green and SVBP is colored light green. Four sulfate ions are shown as spheres and are labeled A–D. Nine α-helices of VASH1c are numbered from the N-terminus to the C-terminus. (b) Comparison of VASH1c–SVBP structures. The VASH1c–SVBP structure was superimposed on the reported crystal structure (PDB entry 6j7b, gray). (c) Sulfate ion (SO42−A) bound in the vicinity of the catalytic triad. Three residues (Tyr134, Ser221 and Arg222) in contact with the sulfate ion are highlighted as stick models and water O atoms are shown as red spheres. (d) The VASH1c–SVBP heterotetramer structure in two orthogonal views. A neighboring crystallographic twofold symmetry-related molecule is shown as a ribbon representation. Chains A and D (green and magenta, respectively) correspond to VASH1c. Chains B and E (light green and pink, respectively) correspond to SVBP. Arg76 of chain A (VASH1c) and Glu28 of chain E (SVBP) that form a hydrogen bond to the symmetry-related molecule are shown as stick models. |
![[Figure 1]](ji5016fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
