Sandbox Reserved 1803: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Victor Kiiza (talk | contribs) No edit summary |
Victor Kiiza (talk | contribs) No edit summary |
||
| Line 43: | Line 43: | ||
The figure shows from the paper shows the crystal structure of LdmS highlighting the location of the P-loop and N-loop motifs. The P-loop motif is shown in <scene name='95/954100/Motifs/2'>Dark</scene>, while the N-loop motif is shown in<scene name='95/954100/Motifs/3'> blue.</scene> | The figure shows from the paper shows the crystal structure of LdmS highlighting the location of the P-loop and N-loop motifs. The P-loop motif is shown in <scene name='95/954100/Motifs/2'>Dark</scene>, while the N-loop motif is shown in<scene name='95/954100/Motifs/3'> blue.</scene> | ||
Dimerization Interface: LdmS exists as a dimer in solution, and dimerization is critical for its enzymatic activity. The dimerization interface involves the formation of a β-sheet between two monomers, which creates a cleft that accommodates the ligand-binding site. The dimerization interface also helps to stabilize the protein structure and protect the active site from solvent exposure. | Dimerization Interface: LdmS exists as a dimer in solution, and dimerization is critical for its enzymatic activity. The dimerization interface involves the formation of a β-sheet<scene name='95/954100/Amino_acids/2'>(blue-violet</scene>) between two monomers, which creates a cleft that accommodates the ligand-binding site. The dimerization interface also helps to stabilize the protein structure and protect the active site from solvent exposure. | ||
