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Literature summary for 7.4.2.5 extracted from

  • Prabudiansyah, I.; Kusters, I.; Driessen, A.J.
    In vitro interaction of the housekeeping SecA1 with the accessory SecA2 protein of Mycobacterium tuberculosis (2015), PLoS ONE, 10, e0128788.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGP3 subunit SecA2
-
Mycobacterium tuberculosis P9WGP5 subunit SecA1
-
Mycobacterium tuberculosis H37Rv P9WGP3 subunit SecA2
-
Mycobacterium tuberculosis H37Rv P9WGP5 subunit SecA1
-

Subunits

Subunits Comment Organism
dimer subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer Mycobacterium tuberculosis
dimer subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer Mycobacterium tuberculosis