1z5q

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1z5q.png|left|200px]]
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==NMR BASED STRUCTURAL MODEL OF THE SUMO-3/UBC9 COMPLEX==
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<StructureSection load='1z5q' size='340' side='right'caption='[[1z5q]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1z5q| PDB=1z5q | SCENE= }}
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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>
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===NMR BASED STRUCTURAL MODEL OF THE SUMO-3/UBC9 COMPLEX===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16224784}}
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<div class="pdbe-citations 1z5q" style="background-color:#fffaf0;"></div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016224784</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Theoretical Model]]
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[[Category: Large Structures]]
[[Category: Ding, H]]
[[Category: Ding, H]]
[[Category: Liu, H]]
[[Category: Liu, H]]

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

NMR BASED STRUCTURAL MODEL OF THE SUMO-3/UBC9 COMPLEX

PDB ID 1z5q

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