2ayn: Difference between revisions

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[[Image:2ayn.png|left|200px]]


{{STRUCTURE_2ayn| PDB=2ayn | SCENE= }}
==Structure of USP14, a proteasome-associated deubiquitinating enzyme==
<StructureSection load='2ayn' size='340' side='right'caption='[[2ayn]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ayn]] 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=2AYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYN 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]] 3.2&#8491;</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=2ayn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayn OCA], [https://pdbe.org/2ayn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ayn RCSB], [https://www.ebi.ac.uk/pdbsum/2ayn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ayn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBP14_HUMAN UBP14_HUMAN] Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).<ref>PMID:18162577</ref> <ref>PMID:19135427</ref> <ref>PMID:19106094</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/2ayn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ayn ConSurf].
<div style="clear:both"></div>


===Structure of USP14, a proteasome-associated deubiquitinating enzyme===
==See Also==
 
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
{{ABSTRACT_PUBMED_16211010}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2ayn]] is a 3 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=2AYN OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:016211010</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitin thiolesterase]]
[[Category: Large Structures]]
[[Category: Hu, M.]]
[[Category: Hu M]]
[[Category: Jeffrey, P D.]]
[[Category: Jeffrey PD]]
[[Category: Li, P.]]
[[Category: Li P]]
[[Category: Shi, Y.]]
[[Category: Shi Y]]
[[Category: Deubiquitinating enzyme]]
[[Category: Dub]]
[[Category: Enzyme mechanism]]
[[Category: Hydrolase]]
[[Category: Proteasome]]
[[Category: Usp14]]

Latest revision as of 12:14, 14 February 2024

Structure of USP14, a proteasome-associated deubiquitinating enzymeStructure of USP14, a proteasome-associated deubiquitinating enzyme

Structural highlights

2ayn is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UBP14_HUMAN Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Koulich E, Li X, DeMartino GN. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol Biol Cell. 2008 Mar;19(3):1072-82. Epub 2007 Dec 27. PMID:18162577 doi:http://dx.doi.org/10.1091/mbc.E07-10-1040
  2. Nagai A, Kadowaki H, Maruyama T, Takeda K, Nishitoh H, Ichijo H. USP14 inhibits ER-associated degradation via interaction with IRE1alpha. Biochem Biophys Res Commun. 2009 Feb 20;379(4):995-1000. doi:, 10.1016/j.bbrc.2008.12.182. Epub 2009 Jan 9. PMID:19135427 doi:http://dx.doi.org/10.1016/j.bbrc.2008.12.182
  3. Mines MA, Goodwin JS, Limbird LE, Cui FF, Fan GH. Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK ativation. J Biol Chem. 2009 Feb 27;284(9):5742-52. doi: 10.1074/jbc.M808507200. Epub 2008, Dec 23. PMID:19106094 doi:http://dx.doi.org/10.1074/jbc.M808507200

2ayn, resolution 3.20Å

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