4ae4: Difference between revisions
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New page: '''Unreleased structure''' The entry 4ae4 is ON HOLD Authors: Agromayor, M., Soler, N., Caballe, A., Kueck, T., Freund, S.M., Allen, M.D., Bycroft, M., Perisic, O., Ye, Y., McDonald, B.... |
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The | ==The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a novel SOUBA domain== | ||
<StructureSection load='4ae4' size='340' side='right'caption='[[4ae4]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ae4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AE4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=MSO:SELENOMETHIONINE+SELENOXIDE'>MSO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wgn|1wgn]]</div></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=4ae4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ae4 OCA], [https://pdbe.org/4ae4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ae4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ae4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ae4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). NMR analysis shows that each of the three rigidly arranged overlapping UBAs making up the SOUBA interact with ubiquitin. We demonstrate that UBAP1-containing ESCRT-I is essential for degradation of antiviral cell-surface proteins, such as tetherin (BST-2/CD317), by viral countermeasures, namely, the HIV-1 accessory protein Vpu and the Kaposi sarcoma-associated herpesvirus (KSHV) ubiquitin ligase K5. | |||
The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain.,Agromayor M, Soler N, Caballe A, Kueck T, Freund SM, Allen MD, Bycroft M, Perisic O, Ye Y, McDonald B, Scheel H, Hofmann K, Neil SJ, Martin-Serrano J, Williams RL Structure. 2012 Mar 7;20(3):414-28. PMID:22405001<ref>PMID:22405001</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ae4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Agromayor, M]] | |||
[[Category: Allen, M D]] | |||
[[Category: Bycroft, M]] | |||
[[Category: Caballe, A]] | |||
[[Category: Freund, S M]] | |||
[[Category: Hofmann, K]] | |||
[[Category: Kueck, T]] | |||
[[Category: Martin-Serrano, J]] | |||
[[Category: McDonald, B]] | |||
[[Category: Neil, S J.D]] | |||
[[Category: Perisic, O]] | |||
[[Category: Scheel, H]] | |||
[[Category: Soler, N]] | |||
[[Category: Williams, R L]] | |||
[[Category: Ye, Y]] | |||
[[Category: Endosomal sorting]] | |||
[[Category: Hiv-1]] | |||
[[Category: Monoubiquitin]] | |||
[[Category: Protein transport]] | |||
[[Category: Tetherin]] | |||
[[Category: Vpu]] | |||
Latest revision as of 08:31, 25 August 2022
The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a novel SOUBA domainThe UBAP1 subunit of ESCRT-I interacts with ubiquitin via a novel SOUBA domain
Structural highlights
Publication Abstract from PubMedThe endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). NMR analysis shows that each of the three rigidly arranged overlapping UBAs making up the SOUBA interact with ubiquitin. We demonstrate that UBAP1-containing ESCRT-I is essential for degradation of antiviral cell-surface proteins, such as tetherin (BST-2/CD317), by viral countermeasures, namely, the HIV-1 accessory protein Vpu and the Kaposi sarcoma-associated herpesvirus (KSHV) ubiquitin ligase K5. The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain.,Agromayor M, Soler N, Caballe A, Kueck T, Freund SM, Allen MD, Bycroft M, Perisic O, Ye Y, McDonald B, Scheel H, Hofmann K, Neil SJ, Martin-Serrano J, Williams RL Structure. 2012 Mar 7;20(3):414-28. PMID:22405001[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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