Part:BBa_K3381005
Mst-CopC-CBM2a
Mst-CopC-CBM2a is a fusion protein consisting of Mst-CopC, a copper-binding domain, as well as CBM2a, a cellulose-binding domain. A linker sequence that was found to naturally occur in a CBM2a fusion was used as a linker domain between Mst-CopC and CBM2a (Courtade, 2018). The CBM2a and flexible linker sequence was submitted as part BBa_K3381007. Additionally, a sequence for a His-tag as well as a TEV recognition sequence was added to the N-terminus for ease of purification (by immobilized-metal affinity chromatography [IMAC]). Fusion proteins containing cellulose-binding modules (CBMs) have readily been used in industrial purification processes, where the CBMs act as affinity tags. Strikingly enough, waste processing seems to be an application that has not been as fervently explored (Zhou, 2020). Furthermore, current waste processing methods fail to provide a way to recover metal ions once extracted, leaving the playing field open to technologies that make metal recovery possible. Mst-CopC-CBM2a is a fusion protein that allows for extraction and recovery of copper(II) from aqueous waste. It binds irreversibly to cellulose, and can also bind Cu(II) (Koropatkin, 2007). This makes it appropriate for affinity chromatography or related uses. Our molecular dynamics simulation showed that Mst-CopC 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 the engineering and model pages).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 785
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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