EC Number   |
|---|
   3.4.21.53 | 119-amino acid N-terminal domain |
| 3.4.21.53 | AAA+ alpha domain, containing four alpha helices and two parallel strands |
| 3.4.21.53 | carboxy-terminal domain crystallized |
| 3.4.21.53 | contains two transmembrane helices within its N-terminal domain |
| 3.4.21.53 | crystal structure determination at 2.0 A resolution |
| 3.4.21.53 | crystal structure determination of LonB proteolytic domain |
| 3.4.21.53 | deletion mutant lacking the putative membrane-anchoring region, residues 134-170, and introduction of mutations S523A and K566A, to 2.0 A resolution. The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the ATPase domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating ATPase domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts |
| 3.4.21.53 | digestion of lonA by alpha-chymotrypsin yields a stable fragment consisting of residues 491-584 crystallized. Crystal structure of the proteolytic domain of lonA (residues 585-784) elucidates a unique fold, P31 space group |
| 3.4.21.53 | fragment containing the ATPase and protease domains, to 3.4 A resolution. The C-terminal protease domain and the two ATPase sub-domains, form a three-lobed structure, whilst the fourth, the N-terminal domain of the fragment, protrudes from the side of the ATPase domain. A second fragment containing two-thirds of the N-terminal domain, to 2.6 A resolution, shows a domain-swapped dimer in the asymmetric unit. The structure of the N-terminal fragment consists of two distinct regions, connected by an extended loop of 10 amino acids: a compact beta-sheet rich, globular domain. Lon protease complexes may be stabilized by coiled-coil interactions between neighbouring N-terminal domains |
| 3.4.21.53 | inactive Lon-S679A P-domain successfully crystallized by the hanging drop vapor diffusion method |
