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3pt3

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[[Image:3pt3.png|left|200px]]
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==Crystal structure of the C-terminal lobe of the human UBR5 HECT domain==
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<StructureSection load='3pt3' size='340' side='right' caption='[[3pt3]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3pt3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PT3 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBR5, EDD, EDD1, HYD, KIAA0896 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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=3pt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pt3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pt3 RCSB], [http://www.ebi.ac.uk/pdbsum/3pt3 PDBsum]</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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UBR5 ubiquitin ligase (also known as EDD, Rat100 or hHYD) is a member of the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases as it contains a C-terminal HECT domain. In ubiquitination cascades involving E3s of the HECT class, ubiquitin is transferred from an associated E2 ubiquitin-conjugating enzyme to the acceptor cysteine of the HECT domain, which consists of structurally distinct N- and C-lobes connected by a flexible linker. Here, the high-resolution crystal structure of the C-lobe of the HECT domain of human UBR5 is presented. The structure reveals important features that are unique compared with other HECT domains. In particular, a distinct four-residue insert in the second helix elongates this helix, resulting in a strikingly different orientation of the preceding loop. This protruding loop is likely to contribute to specificity towards the E2 ubiquitin-conjugating enzyme UBCH4, which is an important functional partner of UBR5. Ubiquitination assays showed that the C-lobe of UBR5 is able to form a thioester-linked E3-ubiquitin complex, although it does not physically interact with UBCH4 in NMR experiments. This study contributes to a better understanding of UBR5 ubiquitination activity.
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{{STRUCTURE_3pt3| PDB=3pt3 | SCENE= }}
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Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase.,Matta-Camacho E, Kozlov G, Menade M, Gehring K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1158-63., doi: 10.1107/S1744309112036937. Epub 2012 Sep 22. PMID:23027739<ref>PMID:23027739</ref>
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===Crystal structure of the C-terminal lobe of the human UBR5 HECT domain===
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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_23027739}}
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==See Also==
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*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
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==About this Structure==
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== References ==
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[[3pt3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PT3 OCA].
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Gehring, K.]]
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[[Category: Gehring, K]]
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[[Category: Kozlov, G.]]
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[[Category: Kozlov, G]]
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[[Category: Matta-Camacho, E.]]
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[[Category: Matta-Camacho, E]]
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[[Category: Menade, M.]]
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[[Category: Menade, M]]
[[Category: Edd]]
[[Category: Edd]]
[[Category: Hhyd]]
[[Category: Hhyd]]

Revision as of 13:35, 9 December 2014

Crystal structure of the C-terminal lobe of the human UBR5 HECT domain

3pt3, resolution 1.97Å

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