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New page: left|200px<br /> <applet load="2grp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2grp, resolution 2.050Å" /> '''Crystal Structure ...
 
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[[Image:2grp.gif|left|200px]]<br />
<applet load="2grp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2grp, resolution 2.050&Aring;" />
'''Crystal Structure of human RanGAP1-Ubc9-Y87A'''<br />


==Overview==
==Crystal Structure of human RanGAP1-Ubc9-Y87A==
E2 conjugating proteins that transfer ubiquitin and ubiquitin-like, modifiers to substrate lysine residues must first activate the lysine, nucleophile for conjugation. Genetic complementation revealed three side, chains of the E2 Ubc9 that were crucial for normal growth. Kinetic, analysis revealed modest binding defects but substantially lowered, catalytic rates for these mutant alleles with respect to wild-type Ubc9., X-ray structures for wild-type and mutant human Ubc9-RanGAP1 complexes, showed partial loss of contacts to the substrate lysine in mutant, complexes. Computational analysis predicted pK perturbations for the, substrate lysine, and Ubc9 mutations weakened pK suppression through, improper side chain coordination. Biochemical studies with p53, RanGAP1, and the Nup358/RanBP2 E3 were used to determine rate constants and pK, values, confirming both structural and computational predictions. It seems, that Ubc9 uses an indirect mechanism to activate lysine for conjugation, that may be conserved among E2 family members.
<StructureSection load='2grp' size='340' side='right'caption='[[2grp]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2grp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GRP 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]] 2.05&#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=2grp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2grp OCA], [https://pdbe.org/2grp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2grp RCSB], [https://www.ebi.ac.uk/pdbsum/2grp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2grp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBC9_HUMAN UBC9_HUMAN] Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation.<ref>PMID:8668529</ref> <ref>PMID:11451954</ref> <ref>PMID:15809060</ref> <ref>PMID:19744555</ref> <ref>PMID:19638400</ref> <ref>PMID:17466333</ref> <ref>PMID:20077568</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/gr/2grp_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=2grp ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Blood group, Cad system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=111730 111730]], Blood group, Sd system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=111730 111730]]
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
 
== References ==
==About this Structure==
<references/>
2GRP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GRP OCA].
__TOC__
 
</StructureSection>
==Reference==
Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway., Yunus AA, Lima CD, Nat Struct Mol Biol. 2006 Jun;13(6):491-9. Epub 2006 May 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16732283 16732283]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Lima CD]]
[[Category: Lima, C.D.]]
[[Category: Yunus AA]]
[[Category: Yunus, A.A.]]
[[Category: conjugation]]
[[Category: small ubiquitin like modifer]]
[[Category: smt3]]
[[Category: ubiquitin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:21:38 2007''

Latest revision as of 09:29, 14 February 2024

Crystal Structure of human RanGAP1-Ubc9-Y87A

2grp, resolution 2.05Å

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