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Literature summary for 3.4.21.107 extracted from

  • Sun, W.; Gao, F.; Fan, H.; Shan, X.; Sun, R.; Liu, L.; Gong, W.
    The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases (2013), Acta Crystallogr. Sect. D, 69, 830-837.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant S266A, to 2.6 A resolution. The protein trimer contains two calcium ions in a central channel, suggesting a link between photodamage control and calcium ions in chloroplasts. Protein contains no PDZ domain and the trimeric structure reveals a catalytic triad conformation where His147 in the alternative conformation is rotated anticlockwise by 120°, preventing formation of the His147-Asp188 hydrogen bond Arabidopsis thaliana
mutant S292A, to 2.0 A resolution. Isoform Deg8 forms a hexamer in the crystals. The catalytic triad of Deg8 consists of His171, Asp214 and Ser292. In the Deg8 (S292A) structure the triad fails to form catalytically competent hydrogen bonds owing to the anticlockwise rotation of the chi1 angle of His171 by 120°. His171 can form a hydrogen bond to Gln272 of loop L3 Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
S266A mutation introduced to avoid self-degradation during crystallization Arabidopsis thaliana
S292A mutation introduced to avoid self-degradation during crystallization Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
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Arabidopsis thaliana 9507
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9LU10
-
-
Arabidopsis thaliana Q9SEL7
-
-

Synonyms

Synonyms Comment Organism
DEG5
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Arabidopsis thaliana
DEG8
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Arabidopsis thaliana
protease Do-like 5
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Arabidopsis thaliana
protease Do-like 8
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Arabidopsis thaliana