EC Number   |
Subunits |
Reference |
|---|
   7.4.2.5 | dimer |
- |
670487, 687406, 688391 |
| 7.4.2.5 | dimer |
2 * 102000, gel filtration, furthermore electron paramagnetic resonance spectroscopy used to identify the interactive binding surface of SecA |
699554 |
| 7.4.2.5 | dimer |
2 * 34000, SDS-PAGE |
656145 |
| 7.4.2.5 | dimer |
chemical cross-linking experiments, dimerization is necessary for the translocation ATPase activity of SecA, monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector |
698596 |
| 7.4.2.5 | dimer |
covalently dimerized SecA is functional in protein translocation |
669390 |
| 7.4.2.5 | dimer |
is the active form of the enzyme. ATP-promoted dimerization of HlyB-nucleotide binding domain might involve formation of two interconvertible forms: a readily dissociable active dimer and a more stable, reversibly inactive form of the dimer |
667693 |
| 7.4.2.5 | dimer |
membrane-bound SEcA dimer exists and is required for effective protein translocation |
670687 |
| 7.4.2.5 | dimer |
SDS-PAGE (verified by gel filtration) |
698635 |
| 7.4.2.5 | 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 |
-, 735024 |
| 7.4.2.5 | 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 |
-, 735024 |
