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1uch

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(New page: 200px<br /> <applet load="1uch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uch, resolution 1.80&Aring;" /> '''DEUBIQUITINATING EN...)
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[[Image:1uch.gif|left|200px]]<br />
 
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<applet load="1uch" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uch, resolution 1.80&Aring;" />
 
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'''DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION'''<br />
 
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==Overview==
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==DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION==
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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)]]
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<StructureSection load='1uch' size='340' side='right'caption='[[1uch]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uc/1uch_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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]].
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cook, W.J.]]
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[[Category: Cook WJ]]
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[[Category: Hill, C.P.]]
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[[Category: Hill CP]]
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[[Category: Johnston, S.C.]]
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[[Category: Johnston SC]]
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[[Category: Larsen, C.N.]]
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[[Category: Larsen CN]]
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[[Category: Wilkinson, K.D.]]
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[[Category: Wilkinson KD]]
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[[Category: c-terminal hydrolase]]
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[[Category: cysteine protease]]
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[[Category: deubiquitinating enzyme]]
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[[Category: ubiquitin]]
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[[Category: ubiquitin conjugation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:54:16 2007''
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Current revision

DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION

PDB ID 1uch

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