 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 8]](kw5082fig8mag.jpg)
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Figure 8
Various P-loop protein structures exhibit an inactive catalytic site conformation. (a) P-loop superposition of ClpA NBD2 (blue, PDB entry 1r6b ; Xia et al., 2004  ) and ClpB NBD2 (green) in complex with ADP. The closely related AAA+ protein ClpA shows an almost identical catalytic site conformation as ClpB, characterized by a stretched Walker A lysine in NBD2 that contacts carbonyl backbone groups. Notably, the corresponding Walker A lysine in NBD1 of both proteins directly interacts with the nucleotide in the conventional manner, which is shown for ClpB NBD1 (pink, PDB entry 4hse
; Zeymer et al., 2013). (b) P-loop superposition of nucleotide-bound structures of different P-loop proteins: ClpB NBD2 (green), the kinesin family member Kin10 (pink; PDB entry 3pxn
; Cochran et al., 2011), the human GTPase GIMAP2 that controls apoptosis in lymphocytes (yellow; PDB entry 2xtn
; Schwefel et al., 2010) and the DNA mismatch-repair protein MutS (blue; PDB entry 3k0s
; Lebbink et al., 2010). The Walker A lysine residues adopt a stretched conformation and interact with carbonyl backbone groups but not with the nucleotide, thereby stabilizing an open inactive conformation of the catalytic site. |
![[Figure 8]](kw5082fig8.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
