Pyruvate phosphate dikinase: Difference between revisions

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'''The His-domain in the two conformational states of PPDK. His455 is shown in blue spheres:'''[[Image:two_cond.jpg|right|600px]]<br><br><br>
'''The His-domain in the two conformational states of PPDK. His455 is shown in blue spheres:'''[[Image:two_cond.jpg|right|600px]]<br><br><br>


<div style="float:left;padding:3px;">
<br>
<html5media  height="300" width="300" frameborder="0"  allowfullscreen>https://www.youtube.com/embed/hxuBouGfs_4</html5media><br>
<html5media  height="300" width="300" frameborder="0"  allowfullscreen>https://www.youtube.com/embed/hxuBouGfs_4</html5media><br>
You may also [http://youtu.be/hxuBouGfs_4 download] the full High Resolution video.
You may also [http://youtu.be/hxuBouGfs_4 download] the full High Resolution video.
</div>


'''''The movie''' depicts the catalytic reaction involving three in-line phosphotransfers and the accompanied protein conformational transitions. This is a model based on crystal structures of PPDK from '''Clostridium symbiosum''' in the two extreme conformational states shown to the left and of complexes bound to substrate analogs, phosphonopyruvate and 5'-adenylyl-β,γ-imidodiphosphate (AMPPNP). The nucleotide binding subdomains are colored green and blue. The PEP binding domain is colored cyan. The His-domain is colored yellow, and the linker segments that connect the His-domain to the partner domains are colored red. Ligands and the catalytic histidine are depicted in stick models with the atomic color scheme: Carbon – gray, Nitrogen – blue, Oxygen – red, Phosphorous – green, Magnesium – magenta. Note that the reaction pregresses in the movie in the reverse direction; steps 3 and 2 occur first followed by step 1. The movie was created by Kap Lim and osnat Herzberg''<br>
'''''The movie''' depicts the catalytic reaction involving three in-line phosphotransfers and the accompanied protein conformational transitions. This is a model based on crystal structures of PPDK from '''Clostridium symbiosum''' in the two extreme conformational states shown to the left and of complexes bound to substrate analogs, phosphonopyruvate and 5'-adenylyl-β,γ-imidodiphosphate (AMPPNP). The nucleotide binding subdomains are colored green and blue. The PEP binding domain is colored cyan. The His-domain is colored yellow, and the linker segments that connect the His-domain to the partner domains are colored red. Ligands and the catalytic histidine are depicted in stick models with the atomic color scheme: Carbon – gray, Nitrogen – blue, Oxygen – red, Phosphorous – green, Magnesium – magenta. Note that the reaction pregresses in the movie in the reverse direction; steps 3 and 2 occur first followed by step 1. The movie was created by Kap Lim and osnat Herzberg''<br>

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky, Osnat Herzberg, Eran Hodis, Dan Bolser, David Canner, Michal Harel, Alexander Berchansky, Karl Oberholser, Joel L. Sussman