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| | <StructureSection load='2aak' size='340' side='right'caption='[[2aak]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2aak' size='340' side='right'caption='[[2aak]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2aak]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1aak 1aak]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AAK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2aak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1aak 1aak]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAK FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aak OCA], [http://pdbe.org/2aak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aak RCSB], [http://www.ebi.ac.uk/pdbsum/2aak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aak ProSAT]</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=2aak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aak OCA], [https://pdbe.org/2aak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aak RCSB], [https://www.ebi.ac.uk/pdbsum/2aak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aak ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UBC1_ARATH UBC1_ARATH]] Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.<ref>PMID:16339806</ref> <ref>PMID:8386169</ref> | + | [[https://www.uniprot.org/uniprot/UBC1_ARATH UBC1_ARATH]] Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.<ref>PMID:16339806</ref> <ref>PMID:8386169</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[PDB identification code|PDB identification code]] | + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] |
| - | *[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[UBC1_ARATH] Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The x-ray crystal structure of a recombinant ubiquitin-conjugating enzyme (E2) encoded by the UBC1 gene of the plant Arabidopsis thaliana has been determined with the use of multiple isomorphous replacement techniques and refined at 2.4-A resolution by simulated annealing and restrained least-squares. This E2 is an alpha/beta protein, with four alpha-helices and a four-stranded antiparallel beta-sheet. The NH2 and COOH termini, which may be important for interaction with other enzymes and substrates in the ubiquitin-conjugation pathway, are on the opposite side of the molecule from the cysteine residue that binds to the COOH terminus of ubiquitin. This structure should now allow for the rational analysis of E2 function by in vitro mutagenesis and facilitate the effective design of E2s with unique specificities or catalytic functions.
Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).,Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD J Biol Chem. 1992 Jul 25;267(21):15116-21. PMID:1321826[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kraft E, Stone SL, Ma L, Su N, Gao Y, Lau OS, Deng XW, Callis J. Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol. 2005 Dec;139(4):1597-611. PMID:16339806 doi:http://dx.doi.org/139/4/1597
- ↑ Sullivan ML, Vierstra RD. Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+. J Biol Chem. 1993 Apr 25;268(12):8777-80. PMID:8386169
- ↑ Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD. Three-dimensional structure of a ubiquitin-conjugating enzyme (E2). J Biol Chem. 1992 Jul 25;267(21):15116-21. PMID:1321826
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