1z5q
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(New page: '''Theoretical Model''' The entry 1Z5Q is a Theoretical Model titled 'NMR Based Structural Model of the SUMO-3/Ubc9 Complex'. Category:Theoretical Model ''Page seeded by [http://oc...) |
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| - | + | {{Theoretical_model}} | |
| - | + | ==NMR BASED STRUCTURAL MODEL OF THE SUMO-3/UBC9 COMPLEX== | |
| + | <StructureSection load='1z5q' size='340' side='right'caption='[[1z5q]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z5Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z5q FirstGlance], [https://www.ebi.ac.uk/pdbsum/1z5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z5q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The interaction between small ubiquitin-related modifier SUMO and its conjugating-enzyme Ubc9 (E2) is an essential step in SUMO conjugation cascade. However, an experimental structure of such a transient complex is still unavailable. Here, a structural model of SUMO-3-Ubc9 complex was obtained with HADDOCK, combining NMR chemical shift mapping information. Docking calculations were performed using SUMO-3 and Ubc9 structures as input. The resulting complex reveals that the complementary surface electrostatic potentials contribute dominantly to the specific interaction. At the interface, similar numbers of oppositely-charged conserved residues are identified on the respective binding partners. Hydrogen bonds are formed in the vicinity of the interface to stabilize the complex. Comparison of the structure of SUMO-3-Ubc9 complex generated by HADDOCK and the experimental structures in free form indicates that SUMO-3 and Ubc9 maintain their respective fold as a whole after docking. However, the N-terminal helix alpha1 and its subsequent L1 loop of Ubc9 experience sizeable changes upon complex formation. They cooperatively move towards the hydrophilic side of the beta-sheet of SUMO-3. Our observations are consistent with the data from previous Ubc9 mutational analysis and conformational flexibility studies. Together, we have proposed that the SUMO-3-Ubc9 interaction is strongly electrostatically driven and the N terminus of Ubc9 shifts to SUMO-3 to facilitate the interaction. The NMR-based structural model, which provides considerable insights into the molecular basis of the specific SUMO-E2 recognition and interaction, implicates the general interaction mode between SUMO-3 and Ubc9 homologues from yeast to humans. | ||
| - | + | Structural basis for SUMO-E2 interaction revealed by a complex model using docking approach in combination with NMR data.,Ding H, Yang Y, Zhang J, Wu J, Liu H, Shi Y Proteins. 2005 Dec 1;61(4):1050-8. PMID:16224784<ref>PMID:16224784</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1z5q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Theoretical Model]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ding, H]] | ||
| + | [[Category: Liu, H]] | ||
| + | [[Category: Shi, Y]] | ||
| + | [[Category: Wu, J]] | ||
| + | [[Category: Yang, Y]] | ||
| + | [[Category: Zhang, J]] | ||
Current revision
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NMR BASED STRUCTURAL MODEL OF THE SUMO-3/UBC9 COMPLEX
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Categories: Theoretical Model | Large Structures | Ding, H | Liu, H | Shi, Y | Wu, J | Yang, Y | Zhang, J
