Sandbox GGC3: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 44: | Line 44: | ||
(going through changes but math is cool :/)The A8 motif harbors the hinge residue at Lys439 and the antiparallel two stranded β-sheet is directed into the active site of the enzyme. The φ/ψ angles of Lys439 change from −73°/−12° in the structure of wild-type luciferase in the adenylate-forming conformation to −69°/158° in the cross- linked structure.this illustrates that a large component of the conformational change occurs with a rotation of the ψ angle of the hinge residue. Additional torsion angle changes are seen in φ angles for Arg437 and Leu441, although the magnitude of the change is not as large as at the hinge residue Lys439<ref name="Sundlov"/>. | (going through changes but math is cool :/)The A8 motif harbors the hinge residue at Lys439 and the antiparallel two stranded β-sheet is directed into the active site of the enzyme. The φ/ψ angles of Lys439 change from −73°/−12° in the structure of wild-type luciferase in the adenylate-forming conformation to −69°/158° in the cross- linked structure.this illustrates that a large component of the conformational change occurs with a rotation of the ψ angle of the hinge residue. Additional torsion angle changes are seen in φ angles for Arg437 and Leu441, although the magnitude of the change is not as large as at the hinge residue Lys439<ref name="Sundlov"/>. | ||
