1z7l

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[[Image:1z7l.gif|left|200px]]
 
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==Crystal structure of fragment of mouse ubiquitin-activating enzyme==
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The line below this paragraph, containing "STRUCTURE_1z7l", creates the "Structure Box" on the page.
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<StructureSection load='1z7l' size='340' side='right'caption='[[1z7l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z7l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TBR:HEXATANTALUM+DODECABROMIDE'>TBR</scene></td></tr>
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{{STRUCTURE_1z7l| PDB=1z7l | SCENE= }}
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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=1z7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7l OCA], [https://pdbe.org/1z7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7l RCSB], [https://www.ebi.ac.uk/pdbsum/1z7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UBA1_MOUSE UBA1_MOUSE] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.
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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/z7/1z7l_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=1z7l ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of fragment of mouse ubiquitin-activating enzyme'''
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==See Also==
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*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
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__TOC__
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==Overview==
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</StructureSection>
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Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ubiquitin-activating enzyme, there are several ubiquitin-conjugating enzymes, and most ubiquitin-conjugating enzymes can in turn interact with multiple ubiquitin ligases. Despite the central role of ubiquitin-activating enzyme in this cascade, a crystal structure of a ubiquitin-activating enzyme is not available. The enzyme is thought to consist of an adenylation domain, a catalytic cysteine domain, a four-helix bundle, and possibly, a ubiquitin-like domain. Its adenylation domain can be modeled because it is clearly homologous to the structurally known adenylation domains of the activating enzymes for the small ubiquitin-like modifier (SUMO) and for the protein encoded by the neuronal precursor cell-expressed, developmentally down-regulated gene 8 (NEDD8). Low sequence similarity and vastly different domain lengths make modeling difficult for the catalytic cysteine domain that results from the juxtaposition of two catalytic cysteine half-domains. Here, we present a biochemical and crystallographic characterization of the two half-domains and the crystal structure of the larger, second catalytic cysteine half-domain of mouse ubiquitin-activating enzyme. We show that the domain is organized around a conserved folding motif that is also present in the NEDD8- and SUMO-activating enzymes, and we propose a tentative model for full-length ubiquitin-activating enzyme.
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[[Category: Large Structures]]
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==About this Structure==
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1Z7L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7L OCA].
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==Reference==
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Crystal structure of a fragment of mouse ubiquitin-activating enzyme., Szczepanowski RH, Filipek R, Bochtler M, J Biol Chem. 2005 Jun 10;280(23):22006-11. Epub 2005 Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15774460 15774460]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bochtler M]]
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[[Category: Bochtler, M.]]
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[[Category: Filipek R]]
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[[Category: Filipek, R.]]
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[[Category: Szczepanowski RH]]
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[[Category: Szczepanowski, R H.]]
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[[Category: Scch]]
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[[Category: Second catalytic cysteine half-domain]]
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[[Category: Ubiquitin-activating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:16:40 2008''
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Current revision

Crystal structure of fragment of mouse ubiquitin-activating enzyme

PDB ID 1z7l

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