View source for 5iaa


==Crystal structure of human UBA5 in complex with UFM1==
<StructureSection load='5iaa' size='340' side='right'caption='[[5iaa]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iaa]] is a 4 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=5IAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IAA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5iaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iaa OCA], [https://pdbe.org/5iaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iaa RCSB], [https://www.ebi.ac.uk/pdbsum/5iaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iaa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBA5_HUMAN UBA5_HUMAN] E1-like enzyme which activates UFM1 and SUMO2.<ref>PMID:15071506</ref> <ref>PMID:18442052</ref> <ref>PMID:20368332</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Modification of proteins by ubiquitin or ubiquitin-like proteins (UBLs) is a critical cellular process implicated in a variety of cellular states and outcomes. A prerequisite for target protein modification by a UBL is the activation of the latter by activating enzymes (E1s). Here, we present the crystal structure of the non-canonical homodimeric E1, UBA5, in complex with its cognate UBL, UFM1, and supporting biochemical experiments. We find that UBA5 binds to UFM1 via a trans-binding mechanism in which UFM1 interacts with distinct sites in both subunits of the UBA5 dimer. This binding mechanism requires a region C-terminal to the adenylation domain that brings UFM1 to the active site of the adjacent UBA5 subunit. We also find that transfer of UFM1 from UBA5 to the E2, UFC1, occurs via a trans mechanism, thereby requiring a homodimer of UBA5. These findings explicitly elucidate the role of UBA5 dimerization in UFM1 activation.

Trans-Binding Mechanism of Ubiquitin-like Protein Activation Revealed by a UBA5-UFM1 Complex.,Oweis W, Padala P, Hassouna F, Cohen-Kfir E, Gibbs DR, Todd EA, Berndsen CE, Wiener R Cell Rep. 2016 Sep 20;16(12):3113-20. doi: 10.1016/j.celrep.2016.08.067. PMID:27653677<ref>PMID:27653677</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5iaa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ubiquitin-fold modifier|Ubiquitin-fold modifier]]
*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oweis W]]
[[Category: Padala P]]
[[Category: Wiener R]]