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1yov

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[[Image:1yov.gif|left|200px]]<br /><applet load="1yov" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yov, resolution 2.6&Aring;" />
 
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'''Insights into the Ubiquitin Transfer Cascade from the refined structure of the activating enzyme for NEDD8'''<br />
 
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==Overview==
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==Insights into the Ubiquitin Transfer Cascade from the refined structure of the activating enzyme for NEDD8==
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Post-translational modification by ubiquitin-like proteins (Ublps) is an essential cellular regulatory mechanism. The Ublp NEDD8 regulates cell division, signalling and embryogenesis. Ublps are conjugated to their targets by the sequential action of E1, E2 and often E3 enzymes. Each Ublp has a dedicated E1, or activating enzyme, that initiates its conjugation cascade. First, E1 associates with the Ublp and catalyses adenylation of the carboxy terminus of the Ublp. Second, E1 forms a thioester between its catalytic cysteine and the Ublp. Next, E1 is loaded with a second Ublp molecule, adenylating the C terminus of this second Ublp while still carrying the first thioester-bound Ublp. Last, E1 binds E2 and promotes Ublp transfer to the catalytic cysteine of E2. We report here the structure and mutational analysis of human APPBP1-UBA3, the heterodimeric E1 enzyme for NEDD8 (ref. 11). Each E1 activity is specified by a domain: an adenylation domain resembling bacterial adenylating enzymes, an E1-specific domain organized around the catalytic cysteine, and a domain involved in E2 recognition resembling ubiquitin. The domains are arranged around two clefts that coordinate protein and nucleotide binding so that each of E1's reactions drives the next, in an assembly-line fashion.
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<StructureSection load='1yov' size='340' side='right'caption='[[1yov]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yov]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ngv 1ngv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YOV 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]] 2.6&#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=ZN:ZINC+ION'>ZN</scene></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=1yov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yov OCA], [https://pdbe.org/1yov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yov RCSB], [https://www.ebi.ac.uk/pdbsum/1yov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yov ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UBA3_HUMAN UBA3_HUMAN] Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.<ref>PMID:10207026</ref> <ref>PMID:9694792</ref> <ref>PMID:12740388</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/yo/1yov_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=1yov 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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1YOV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1NGV. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOV OCA].
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*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
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== References ==
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==Reference==
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<references/>
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Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8., Walden H, Podgorski MS, Schulman BA, Nature. 2003 Mar 20;422(6929):330-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12646924 12646924]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Podgorski, M S.]]
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[[Category: Podgorski MS]]
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[[Category: Schulman, B A.]]
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[[Category: Schulman BA]]
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[[Category: Walden, H.]]
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[[Category: Walden H]]
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[[Category: ZN]]
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[[Category: appbp1]]
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[[Category: e1]]
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[[Category: nedd8]]
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[[Category: uba3]]
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[[Category: ubiquitin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:35 2008''
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Current revision

Insights into the Ubiquitin Transfer Cascade from the refined structure of the activating enzyme for NEDD8

PDB ID 1yov

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