Difference between revisions of "Part:BBa K3381002"

Latest revision as of 01:29, 24 October 2020

Mst-CopC (copper-binding)

Mst-CopC is a copper binding protein with a single binding site that preferentially binds Cu(II). Published binding affinities for Mst-CopC did not include the variant present in Methylosinus trichosporium; however, our molecular dynamics simulation showed that it had a total interaction energy of -540.64 KJ/mol. This was done with a 10 nanosecond simulation using GROMACS and the Charmm36 force field (Vanommeslaeghe, 2010) (see our engineering and model pages for more information). Mst-CopC binds Cu(II) with a “distorted square pyramidal geometry with H23, H107, D105, and the amino terminus comprising the planar ligands and a water molecule serving as the axial ligand” (Lawton, Kenney, Hurley, & Rosenzweig, 2016).

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K3381002 short</partinfo>
-Mst-CopC is a copper binding protein with a single binding site that preferentially binds Cu(II). Published binding affinities for Mst-CopC did not include the variant present in Methylosinus trichosporium; however, we determined its interaction energy was -540.6373 kJ/mol using molecular dynamics. Mst-CopC binds Cu(II) with a “distorted square pyramidal geometry with H23, H107, D105, and the amino terminus comprising the planar ligands and a water molecule serving as the axial ligand” (Lawton, Kenney, Hurley, & Rosenzweig, 2016).
+Mst-CopC is a copper binding protein with a single binding site that preferentially binds Cu(II). Published binding affinities for Mst-CopC did not include the variant present in Methylosinus trichosporium; however, our molecular dynamics simulation showed that it had a total interaction energy of -540.64 KJ/mol. This was done with a 10 nanosecond simulation using GROMACS and the Charmm36 force field (Vanommeslaeghe, 2010) (see our [https://2020.igem.org/Team:Waterloo/Engineering engineering] and [https://2020.igem.org/Team:Waterloo/Model model] pages for more information). Mst-CopC binds Cu(II) with a “distorted square pyramidal geometry with H23, H107, D105, and the amino terminus comprising the planar ligands and a water molecule serving as the axial ligand” (Lawton, Kenney, Hurley, & Rosenzweig, 2016).
 <!-- Add more about the biology of this part here