Crystallization (Comment) | Organism |
---|---|
solution structure of fully active, recombinant GLuc. GLuc is an all-alphahelix protein made of nine helices. Two homologous sequential repeats form two anti-parallel bundles made by 4 helices and tied together by three disulfide bonds. The N-terminal helix 1 is grabbed by these 4 helices | Gaussia princeps |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gaussia princeps | Q9BLZ2 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
side-chain modification | natively folded GLuc possesses ten cysteines that form five disulfide bonds. Bonding occurs at C59/C120, C65/C77, and C136/C148. Additionally, C52/C127 and C56/C123 are the most favored pairs | Gaussia princeps |
Purification (Comment) | Organism |
---|---|
natively folded GLuc is obtained by bacterial expression and efficient refolding using a solubility enhancement petide tag | Gaussia princeps |
Subunits | Comment | Organism |
---|---|---|
? | x * 19062, MALDI-TOF, x * 19056, calcuated from sequence | Gaussia princeps |
Synonyms | Comment | Organism |
---|---|---|
GLuc | - |
Gaussia princeps |