Receiver domain of sensor histidine kinase CKI1: Difference between revisions
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Magnesium binding mediates slight structural changes of the active site. Upon magnesium binding, the side chain of the D1050 rotates by app. 90° toward the divalent cation. The connection via salt bridge between D1050 and K1105 induces the rotation of K1105, whereas the salt bridge remains established. | Magnesium binding mediates slight structural changes of the active site. Upon magnesium binding, the side chain of the D1050 rotates by app. 90° toward the divalent cation. The connection via salt bridge between D1050 and K1105 induces the rotation of K1105, whereas the salt bridge remains established. | ||
More, the NMR analysis shows magnesium binding to stabilize conformational flexibility of the loop L3 in the solution (Pekarova, 2011). | More, the NMR analysis shows magnesium binding to stabilize conformational flexibility of the loop L3 in the solution (Pekarova, 2011). | ||
[[Image:Structural and sequentional conservation among receiver domains.png.PNG|250px|right|thumb| Structural and sequential conservation among receiver domains.png.PNG.]] | |||
== 3D Structures of CKI1RD == | == 3D Structures of CKI1RD == | ||