SUMO: Difference between revisions

The <scene name='3kyc/Al/2'>structural alignment</scene> of the crystal structures for human SUMO E1 in complex with SUMO adenylate (AMSN) and tetrahedral intermediate (AVSN) analogues revealed opened conformation (<font color='orange'><b>SUMO1 in orange</b></font>, <font color='blue'><b>SAE1 colored in blue</b></font>, and <font color='darkviolet'><b>other domains in darkviolet</b></font>) and closed conformation (<font color='yellow'><b>SUMO1 in yellow</b></font>, <font color='cyan'><b>SAE1 colored in cyan</b></font>, and <font color='magenta'><b>other domains in magenta</b></font>), respectively. In the <scene name='3kyc/Al/7'>open conformation</scene> ([[3kyc]]) the distance between Cys domain (including Cys173) and mimic of the acyl adenylate intermediate AMSN is very long, while in the <scene name='3kyc/Al/6'>closed conformation</scene> ([[3kyd]]), the catalytic Cys173 is posioned near AVSN and SUMO1, so the overall structure revealed dramatic rearrangement. This large conformational change forms the <scene name='3kyc/Al/8'>E1~SUMO1-AVSN tetrahedral intermediate analogue</scene>.<ref>PMID:20164921</ref>  

For better understanding of the difference between these two conformations you can see this [[Morphs|morph]] (generated by using [http://polyview.cchmc.org/polyview3d.html POLYVIEW-3D: http://polyview.cchmc.org/polyview3d.html]; reload/refresh this page to restart this movie). Of note, in contrast to the previous figure, the same domains of these two structures ([[3kyc]] and [[3kyd]]) are colored in the same colors (<font color='yellow'><b>SUMO1 in yellow</b></font>, <font color='blue'><b>SAE1 colored in blue</b></font> and <font color='darkviolet'><b>other domains in darkviolet</b></font>). The catalytic Cys173 is shown in the spacefill representation and colored green, AMSN (or AVSN) are shown in the spacefill representation and colored in CPK colors.

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