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[[Image:2aak.gif|left|200px]]<br />
<applet load="2aak" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2aak, resolution 2.40&Aring;" />
'''UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA'''<br />


==Overview==
==UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?1321826 (full description)]]
<StructureSection load='2aak' size='340' side='right'caption='[[2aak]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2aak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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>
== Function ==
[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 ==
[[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/aa/2aak_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=2aak ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2AAK is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]]. This structure superseeds the now removed PDB entry 1AAK. Active as [[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]]. Structure known Active Site: C88. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AAK OCA]].
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1321826 1321826]
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Cook WJ]]
[[Category: Cook, W.J.]]
[[Category: Jeffrey LC]]
[[Category: Jeffrey, L.C.]]
[[Category: Sullivan ML]]
[[Category: Sullivan, M.L.]]
[[Category: Vierstra RD]]
[[Category: Vierstra, R.D.]]
[[Category: ligase]]
[[Category: ubiquitin conjugation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:37:53 2007''

Latest revision as of 12:12, 14 February 2024

UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANAUBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA

Structural highlights

2aak is a 1 chain structure with sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 1aak. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. 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
  2. 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

2aak, resolution 2.40Å

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