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Literature summary for 3.4.21.53 extracted from

  • Lin, C.C.; Su, S.C.; Su, M.Y.; Liang, P.H.; Feng, C.C.; Wu, S.H.; Chang, C.I.
    Structural insights into the allosteric operation of the Lon AAA+ protease (2016), Structure, 24, 667-675 .
    View publication on PubMed
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
additional information stimulation of ATPase activity by substrates Meiothermus taiwanensis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified mutant core-E423Q in complex with Mg2+, X-ray diffraction structure determination and analysis Meiothermus taiwanensis

Protein Variants

Protein Variants Comment Organism
E423Q site-directed mutagenesis, mutation of the conserved catalytic glutamate 423 in Walker B motif treatment of Core-E423Q with Mg2+ induces the formation of the open-chambered hexamer. In the crystal, each asymmetric unit contains one hexameric assembly, with three non-neighboring protomers (B/D/F) bound to ADP and the other three (A/C/E) nucleotide free. The bound nucleotide is identified as ADP, which may have resulted from spontaneous hydrolysis of ATP. Each Core-E423Q protomer forms an alpha/beta domain capped with a distinct N-terminal three-helix bundle, a middle a domain, and a C-terminal PD, which are together organized into an elongated structure. Six LonA protomers are packed against one another like an orange's carpels and assembled into a cupcake-shaped complex Meiothermus taiwanensis
additional information several truncated constructs of Meiothermus taiwanensis LonA (MtaLonA) without the LAN domain are prepared for crystallization. The DELTAhairpin mutant loses allosteric stimulation of ATPase activity by substrate or inhibitor. DELTALoop-2 mutant, which can degrade casein but has a defective Ig2-translocating activity, shows a wild-type-like ATPase stimulation by casein, but the mutant exhibits a severely reduced ATPase allostery by Ig2 Meiothermus taiwanensis
R536/R584 paddle-like movement of R536/R584 induced by the ATPase cycle at the groove may play an important role in substrate degradation Meiothermus taiwanensis
R563A site-directed mutagenesis Meiothermus taiwanensis
R584A site-directed mutagenesis Meiothermus taiwanensis

Organism

Organism UniProt Comment Textmining
Meiothermus taiwanensis
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-
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Synonyms

Synonyms Comment Organism
Lon AAA+ protease
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 Meiothermus taiwanensis
lonA
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 Meiothermus taiwanensis
MtaLonA
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 Meiothermus taiwanensis

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, stimulation of ATPase activity by substrates. The ATPase cycle of the basic residue(s) adjoining the substrate-binding groove of LonA is involved in substrate degradation Meiothermus taiwanensis

General Information

General Information Comment Organism
additional information the translational and rotational movements in the AAA+ module induced by the nucleotide have a profound impact on the Arg finger Arg484 location and P-loop conformation in ATPase sites. In the nucleotide-free state, the P loop is in an open conformation. In contrast, in the ADP-bound state, the P loop is well formed to accommodate the bound nucleotide Meiothermus taiwanensis
physiological function the Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation Meiothermus taiwanensis