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The effect of the G369E mutation on the structure of BCKDK protein is shown.

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posted on 29.07.2016, 12:19 by J. Samuel Zigler Jr., Colin A. Hodgkinson, Megan Wright, Andrew Klise, Olof Sundin, Karl W. Broman, Fielding Hejtmancik, Hao Huang, Bonnie Patek, Yuri Sergeev, Stacey Hose, Cory Brayton, Jiao Xaiodong, David Vasquez, Nicholas Maragakis, Susumu Mori, David Goldman, Ahmet Hoke, Debasish Sinha

The prediction is based on homology modeling of the structures of BCKDK and the G369E mutant as refined using the 7.5 ns molecular dynamics and shown in beige and light blue, respectively. In the mutant, the helix containing residue E369 is moving outward from the ADP binding site due to repulsion from the negatively charged residue E275. This might suggest a decrease in ADP binding activity by the mutant enzyme due to the replacement of glycine in normal BCKDK by the negatively charged glutamic acid in the mutant variant.

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