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New page: left|200px<br /> <applet load="1uch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uch, resolution 1.80Å" /> '''DEUBIQUITINATING EN...
 
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[[Image:1uch.gif|left|200px]]<br />
<applet load="1uch" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1uch, resolution 1.80&Aring;" />
'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''<br />


==Overview==
==DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION==
Ubiquitin C-terminal hydrolases catalyze the removal of adducts from the, C-terminus of ubiquitin. We have determined the crystal structure of the, recombinant human Ubiquitin C-terminal Hydrolase (UCH-L3) by X-ray, crystallography at 1.8 A resolution. The structure is comprised of a, central antiparallel beta-sheet flanked on both sides by alpha-helices., The beta-sheet and one of the helices resemble the well-known papain-like, cysteine proteases, with the greatest similarity to cathepsin B. This, similarity includes the UCH-L3 active site catalytic triad of Cys95, His169 and Asp184, and the oxyanion hole residue Gln89. Papain and UCH-L3, differ, however, in strand and helix connectivity, which in the UCH-L3, structure includes a disordered 20 residue loop (residues 147-166) that is, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9233788 (full description)]]
<StructureSection load='1uch' size='340' side='right'caption='[[1uch]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1uch]] is a 1 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=1UCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCH 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]] 1.8&#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=1uch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uch OCA], [https://pdbe.org/1uch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uch RCSB], [https://www.ebi.ac.uk/pdbsum/1uch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uch ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UCHL3_HUMAN UCHL3_HUMAN] Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.<ref>PMID:2530630</ref> <ref>PMID:9790970</ref> <ref>PMID:19154770</ref> <ref>PMID:21762696</ref> <ref>PMID:22689415</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/uc/1uch_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=1uch ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1UCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UCH OCA]].
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution., Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP, EMBO J. 1997 Jul 1;16(13):3787-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9233788 9233788]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cook, W.J.]]
[[Category: Cook WJ]]
[[Category: Hill, C.P.]]
[[Category: Hill CP]]
[[Category: Johnston, S.C.]]
[[Category: Johnston SC]]
[[Category: Larsen, C.N.]]
[[Category: Larsen CN]]
[[Category: Wilkinson, K.D.]]
[[Category: Wilkinson KD]]
[[Category: c-terminal hydrolase]]
[[Category: cysteine protease]]
[[Category: deubiquitinating enzyme]]
[[Category: ubiquitin]]
[[Category: ubiquitin conjugation]]
 
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