Journal:Acta Cryst D:S2059798320013510
From Proteopedia
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In the present work, the refinement of the JK-loop is obtained for the first time by X-ray diffraction experiment, thanks to its crystal packing mode. To support the X-ray observation, Molecular Dynamics trajectories are also carried out to provide a dynamical information about the loop in the presence of the cofactor. Such new structural and dynamical information highlights the importance of the JK-loop in confining the labile heme cofactor into the active site. | In the present work, the refinement of the JK-loop is obtained for the first time by X-ray diffraction experiment, thanks to its crystal packing mode. To support the X-ray observation, Molecular Dynamics trajectories are also carried out to provide a dynamical information about the loop in the presence of the cofactor. Such new structural and dynamical information highlights the importance of the JK-loop in confining the labile heme cofactor into the active site. | ||
| - | *<scene name='86/865040/Cv/ | + | *<scene name='86/865040/Cv/13'>Global conformation of JK-loop from crystal structure</scene>. |
*<scene name='86/865040/Cv/8'>Surface into the active site caused by the intermediate conformation of the JK-loop</scene>. This surface is important in order to support the role playing by the JK-loop. | *<scene name='86/865040/Cv/8'>Surface into the active site caused by the intermediate conformation of the JK-loop</scene>. This surface is important in order to support the role playing by the JK-loop. | ||
Revision as of 14:57, 22 October 2020
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