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Literature summary for 2.4.1.16 extracted from

  • Weiss, I.M.; Lueke, F.; Eichner, N.; Guth, C.; Clausen-Schaumann, H.
    On the function of chitin synthase extracellular domains in biomineralization (2013), J. Struct. Biol., 183, 216-225.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
comparative sequence analysis, cloning and expression of the enzyme's transmembrane segment ArCS1_E22TM, recombinant expression of the His-tagged domain in Dictyostelium discoideum, the corresponding transmembrane protein ArCS1_E22TM accumulates in membrane fractions of the expression host Dictyostelium discoideum, recombinant expression of clone EIIIab containing the ArCS1_E22 cDNA fragment in Escherichia coli strain BL21(DE3) Atrina rigida

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane assembly mechanism of the chitin synthase Ar-CS1 via its extracellular domain ArCS1_E22 Atrina rigida 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Atrina rigida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
size analysis of proteins purified at pH 4.7, pH 6.5, and pH 7.5 by using gel filtration, native PAGE, and dynamic light scattering Atrina rigida
13500
-
x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE Atrina rigida
21500
-
x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE Atrina rigida
40000 66000 purified recombinant enzyme, gel filtration Atrina rigida

Organism

Organism UniProt Comment Textmining
Atrina rigida Q288C6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged transmembrane protein ArCS1_E22TM from Dictyostelium discoideum by nickel affinity chromatography, soluble recombinant ArCS1_E22 proteins can be purified as monomers only at basic pH of 9.0 Atrina rigida

Subunits

Subunits Comment Organism
? x * 21500, recombinant transmembrane segment ArCS1_E22, x * 13500, recombinant transmembrane segment ArCS1_E22, SDS-PAGE Atrina rigida
More assembly mechanism of the chitin synthase Ar-CS1 via its extracellular domain ArCS1_E22. ArCS1_E22 forms regular nanostructures on cationic substrates, atomic force microscopy Atrina rigida

Synonyms

Synonyms Comment Organism
Ar-CS1
-
Atrina rigida
CHS
-
Atrina rigida

General Information

General Information Comment Organism
physiological function the extracellular domain ArCS1_E22 is involved in regulating the multiple enzyme activities of Ar-CS1 such as chitin synthesis and myosin movements by interaction with mineral surfaces and eventually by protein assembly. The protein complexes can locally probe the status of mineralization according to pH unless ions and pCO2 are balanced with suitable buffer substances. The intact enzyme can act as a force sensor. The shell formation is coordinated physiologically with precise adjustment of cellular activities to the structure, topography and stiffness at the mineralizing interface Atrina rigida