 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
journal menu
![[Figure 1]](kw5082fig1mag.jpg)
|
|
Figure 1
Model of a typical AAA+ catalytic site in its active conformation. The catalytic site is located at the interface between two neighbouring subunits (red and green) in the oligomeric AAA+ complex. The Walker A lysine, which is crucial for nucleotide binding and catalysis, interacts directly with the phosphates of the bound nucleotide. The essential Mg2+ ion (yellow) is bound between the β- and γ-phosphates of ATP. The Walker B aspartate coordinates the Mg2+ ion (either directly or via the water molecules of the hydration shell). The Walker B glutamate is positioned such that it can activate the attacking water molecule. A conserved catalytically essential arginine residue from the neighbouring subunit (arginine finger) contacts the bound nucleotide. Conserved sensor-motif residues are in close proximity and are involved in nucleotide-state sensing and allosteric communication. This figure was generated based on the structure of the E. coli clamp loader (PDB entry 3glf ; Simonetta et al., 2009  ). Distances are given in Å. Corresponding residues in ClpB NBD2 are listed next to the model. |
![[Figure 1]](kw5082fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
