4y1l
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4y1l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y1L FirstGlance]. <br> | <table><tr><td colspan='2'>[[4y1l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y1L 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=4y1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1l OCA], [https://pdbe.org/4y1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y1l RCSB], [https://www.ebi.ac.uk/pdbsum/4y1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y1l ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=4y1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1l OCA], [https://pdbe.org/4y1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y1l RCSB], [https://www.ebi.ac.uk/pdbsum/4y1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y1l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</ref> | [https://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | An RWD domain is a well-conserved domain found through bioinformatic analysis of the human proteome sequence; however its function has been unknown. Ubiquitin-like modifications require the catalysis of three enzymes generally known as E1, E2 and E3. We solved the crystal structure of the E2 for the small ubiquitin-like modifiers (SUMO) in complex with an RWD domain, and confirmed the structure using solution NMR analysis. RWD's binding surface on Ubc9 is located near the N-terminus of Ubc9 that is known to be involved in non-covalent binding of the proteins in the conjugation machinery, including a domain of E1, SUMO, and an E3 ligase. NMR data indicates that the RWD domain does not bind to SUMO and E1. The interaction between RWD and Ubc9 has a Kd of 32.30+/-3.86 microM. Consistent with the structure and binding affinity and in contrast to a previous report, the RWD domain and RWDD3 have minimal effects on global SUMOylation. The structural and biochemical information presented here forms the basis for further investigation of the functions of RWD containing proteins. | ||
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| - | RWD Domain as an E2 (Ubc9)-Interaction Module.,Alontaga AY, Ambaye ND, Li YJ, Vega R, Chen CH, Bzymek KP, Williams JC, Hu W, Chen Y J Biol Chem. 2015 Apr 27. pii: jbc.M115.644047. PMID:25918163<ref>PMID:25918163</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4y1l" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Ubc9 Homodimer The Missing Link in Poly-SUMO Chain Formation
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Categories: Homo sapiens | Large Structures | Aileen YA | Ambaye ND | Bzymek K | Chen Y | Hu W | Li YJ | Vega R | Williams JC
