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Literature summary for 3.4.21.53 extracted from

  • Duman, R.E.; Loewe, J.
    Crystal structures of Bacillus subtilis Lon protease (2010), J. Mol. Biol., 401, 653-670.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
87400
-
1 * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations Bacillus subtilis
87400
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x * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P37945
-
-

Subunits

Subunits Comment Organism
monomer 1 * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations Bacillus subtilis
oligomer x * 87400, calculated. Mixture of monomeric and larger oligomeric species, with increasing amounts of larger oligomers present at larger concentrations Bacillus subtilis