Journal:Acta Cryst D:S2059798320013510
From Proteopedia
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| - | <StructureSection load='' size='450' side='right' scene=' | + | <StructureSection load='' size='450' side='right' scene='86/865040/Cv/2' caption=''> |
===Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1=== | ===Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine-2,3-dioxygenase-1=== | ||
<big>Mirgaux Manon, Leherte Laurence and Wouters Johan</big> <ref>doi: 10.1107/S2059798320013510</ref> | <big>Mirgaux Manon, Leherte Laurence and Wouters Johan</big> <ref>doi: 10.1107/S2059798320013510</ref> | ||
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In the present work, the refinement of the JK-loop is obatined 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 obatined 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. | ||
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| + | <scene name='86/865040/Cv/1'>Global conformation of JK-loop from crystal structure</scene>. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 15:28, 21 October 2020
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