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| <StructureSection load='6o83' size='340' side='right'caption='[[6o83]], [[Resolution|resolution]] 3.15Å' scene=''> | | <StructureSection load='6o83' size='340' side='right'caption='[[6o83]], [[Resolution|resolution]] 3.15Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6o83]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O83 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6o83]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O83 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VMX:5-{[(3-AMINOPROPYL)SULFONYL]AMINO}-5-DEOXYADENOSINE'>VMX</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.153Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ii3|4ii3]], [[6o82|6o82]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=VMX:5-{[(3-AMINOPROPYL)SULFONYL]AMINO}-5-DEOXYADENOSINE'>VMX</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptr3, SPBC1604.21c, SPBC211.09 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), uep1, ubi2, SPAC1805.12c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=6o83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o83 OCA], [https://pdbe.org/6o83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o83 RCSB], [https://www.ebi.ac.uk/pdbsum/6o83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o83 ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/E1_ubiquitin-activating_enzyme E1 ubiquitin-activating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.45 6.2.1.45] </span></td></tr>
| |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o83 OCA], [http://pdbe.org/6o83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o83 RCSB], [http://www.ebi.ac.uk/pdbsum/6o83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o83 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO]] 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. [[http://www.uniprot.org/uniprot/RL402_SCHPO RL402_SCHPO]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). Ribosomal protein L40 is a component of the 60S subunit of the ribosome. | | [https://www.uniprot.org/uniprot/UBA1_SCHPO UBA1_SCHPO] 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. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6o83" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6o83" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: E1 ubiquitin-activating enzyme]]
| |
| [[Category: Fission yeast]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Hann, Z S]] | | [[Category: Schizosaccharomyces pombe 972h-]] |
| [[Category: Lima, C D]]
| | [[Category: Hann ZS]] |
| [[Category: Adenylation]]
| | [[Category: Lima CD]] |
| [[Category: Atp-binding]]
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| [[Category: Inhibitor]] | |
| [[Category: Isopeptide bond]] | |
| [[Category: Ligase]]
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| [[Category: Ligase-protein binding complex]]
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| [[Category: Nucleotide-binding]]
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| [[Category: Nucleus]]
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| [[Category: Phosphoprotein]]
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| [[Category: Tetrahedral intermediate]]
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| [[Category: Thioester]]
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| [[Category: Ubl conjugation pathway]]
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