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[[Image:2z6p.gif|left|200px]]
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{{STRUCTURE_2z6p|  PDB=2z6p  |  SCENE=  }}
'''Crystal Structure of the Ufc1, Ufm1 conjugating enzyme 1'''


==Crystal Structure of the Ufc1, Ufm1 conjugating enzyme 1==
<StructureSection load='2z6p' size='340' side='right'caption='[[2z6p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2z6p]] is a 1 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=2Z6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z6P FirstGlance]. <br>
</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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z6o|2z6o]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UFC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></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=2z6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6p OCA], [https://pdbe.org/2z6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z6p RCSB], [https://www.ebi.ac.uk/pdbsum/2z6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z6p ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/UFC1_HUMAN UFC1_HUMAN]] E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage.<ref>PMID:15071506</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/z6/2z6p_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=2z6p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.


==Overview==
Crystal structure of Ufc1, the Ufm1-conjugating enzyme.,Mizushima T, Tatsumi K, Ozaki Y, Kawakami T, Suzuki A, Ogasahara K, Komatsu M, Kominami E, Tanaka K, Yamane T Biochem Biophys Res Commun. 2007 Nov 3;362(4):1079-84. Epub 2007 Aug 30. PMID:17825256<ref>PMID:17825256</ref>
Ubiquitin and ubiquitin-like protein-conjugating enzymes play central roles in posttranslational modification processes. The ubiquitin-fold modifier 1 (Ufm1), one of a variety of ubiquitin-like modifiers, is covalently attached to target proteins via Uba5 and Ufm1-conjugating enzyme 1 (Ufc1), which are analogous to the E1 and E2 ubiquitylation enzymes. As Ufm1-related proteins are conserved in metazoa and plants, the Ufm1 system likely plays important roles in various multicellular organisms. Herein, we report the X-ray structure of human Ufc1 determined at 1.6 A resolution. The Ufc1 structure comprises a canonical E2 domain and an additional N-terminal domain. The Uba5 binding site on Ufc1 was assigned by structural comparison of Ufc1 and Ubc12 and related mutational analyses. In addition, we show that the N-terminal unique domain of Ufc1 contributes to thermal stability.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2Z6P is a [[Single protein]] structure of 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=2Z6P OCA].
</div>
<div class="pdbe-citations 2z6p" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of Ufc1, the Ufm1-conjugating enzyme., Mizushima T, Tatsumi K, Ozaki Y, Kawakami T, Suzuki A, Ogasahara K, Komatsu M, Kominami E, Tanaka K, Yamane T, Biochem Biophys Res Commun. 2007 Nov 3;362(4):1079-84. Epub 2007 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825256 17825256]
*[[Ubiquitin-fold modifier|Ubiquitin-fold modifier]]
[[Category: Homo sapiens]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Kawakami, T.]]
[[Category: Kawakami, T]]
[[Category: Komatsu, M.]]
[[Category: Komatsu, M]]
[[Category: Kominami, E.]]
[[Category: Kominami, E]]
[[Category: Mizushima ,T.]]
[[Category: Mizushima , T]]
[[Category: Ogasahara, K.]]
[[Category: Ogasahara, K]]
[[Category: Ozaki, Y.]]
[[Category: Ozaki, Y]]
[[Category: Suzuki, A.]]
[[Category: Suzuki, A]]
[[Category: Tanaka, K.]]
[[Category: Tanaka, K]]
[[Category: Tatsumi, K.]]
[[Category: Tatsumi, K]]
[[Category: Yamane, T.]]
[[Category: Yamane, T]]
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Polymorphism]]
[[Category: Polymorphism]]
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[[Category: Ufc1]]
[[Category: Ufc1]]
[[Category: Ufm1]]
[[Category: Ufm1]]
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