View source for 6h78


==E1 enzyme for ubiquitin like protein activation.==
<StructureSection load='6h78' size='340' side='right'caption='[[6h78]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6h78]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H78 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBA5, UBE1DC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h78 OCA], [http://pdbe.org/6h78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h78 RCSB], [http://www.ebi.ac.uk/pdbsum/6h78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h78 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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 the ubiquitin-like protein, UFM1, requires activation of UFM1 by the E1-activating enzyme, UBA5. In humans, UBA5 possesses two isoforms, each comprising an adenylation domain, but only one containing an N-terminal extension. Currently, the role of the N-terminal extension in UFM1 activation is not clear. Here we provide structural and biochemical data on UBA5 N-terminal extension to understand its contribution to UFM1 activation. The crystal structures of the UBA5 long isoform bound to ATP with and without UFM1 show that the N-terminus not only is directly involved in ATP binding but also affects how the adenylation domain interacts with ATP. Surprisingly, in the presence of the N-terminus, UBA5 no longer retains the 1:2 ratio of ATP to UBA5, but rather this becomes a 1:1 ratio. Accordingly, the N-terminus significantly increases the affinity of ATP to UBA5. Finally, the N-terminus, although not directly involved in the E2 binding, stimulates transfer of UFM1 from UBA5 to the E2, UFC1.

An N-Terminal Extension to UBA5 Adenylation Domain Boosts UFM1 Activation: Isoform-Specific Differences in Ubiquitin-like Protein Activation.,Soudah N, Padala P, Hassouna F, Kumar M, Mashahreh B, Lebedev AA, Isupov MN, Cohen-Kfir E, Wiener R J Mol Biol. 2019 Feb 1;431(3):463-478. doi: 10.1016/j.jmb.2018.10.007. Epub 2018 , Nov 6. PMID:30412706<ref>PMID:30412706</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6h78" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ubiquitin activating enzyme|Ubiquitin activating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Cohen-Kfir, E]]
[[Category: Hassouna, F]]
[[Category: Isupov, M N]]
[[Category: Lebedev, A A]]
[[Category: Mashahreh, B]]
[[Category: Padala, P]]
[[Category: Soudah, N]]
[[Category: Wiener, R]]
[[Category: Transferase]]
[[Category: Ubiquitin like protein activating enzyme]]