journal menu
![[Figure 4]](dw5156fig4mag.jpg)
|
|
Figure 4
Asp187 and its involvement in subunit interactions, with hydrogen bonds shown as dashed lines. (a) A general view of muscle FBPase in the R state, with the two leucine locks between the upper and lower dimers boxed. (b) Residues at the interface of subunits C1–C3 in the R state participating in the formation of the leucine lock. The Asp187 residues from subunit C1 (green) and from subunit C3 (yellow) are shown in ball-and-stick representation in 2Fo − Fc electron density contoured at the 1.0σ level. (c) A general view of muscle FBPase in the T state, with residues at the interface of subunits C1·C2 and C3·C4 boxed. (d) Residues at the interface of subunits C1·C2 in the T state participating in the stabilization of loop L2 in the disengaged position. Asp187 (ball-and-stick representation) from subunit C1 (green) is shown in 2Fo − Fc electron density contoured at the 1.0σ level. Ala51, Gly52, Leu53 and Ala54 from subunit C2 are shown in blue. |
![[Figure 4]](dw5156fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
