1u9b: Difference between revisions

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-[[Image:1u9b.gif|left|200px]]<br />
-<applet load="1u9b" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1u9b, resolution 2.0&Aring;" />
-'''MURINE/HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9'''<br />
-==Overview==
+==MURINE/HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9==
-Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of, Saccharomyces cerevisiae Ubc9 that is essential for the viability of yeast, cells with a specific role in the G2-M transition of the cell cycle. The, structure of recombinant mammalian Ubc9 has been determined from two, crystal forms at 2.0 A resolution. Like Arabidopsis thaliana Ubc1 and S., cerevisiae Ubc4, murine/human Ubc9 was crystallized as a monomer, suggesting that previously reported hetero- and homo-interactions among, Ubcs may be relatively weak or indirect. Compared with the known crystal, structures of Ubc1 and Ubc4, which regulate different cellular processes, Ubc9 has a 5-residue insertion that forms a very exposed tight, beta-hairpin and a 2-residue insertion that forms a bulge in a loop close, to the active site. Mammalian Ubc9 also possesses a distinct electrostatic, potential distribution that may provide possible clues to its remarkable, ability to interact with other proteins. The 2-residue insertion and other, sequence and structural heterogeneity observed at the catalytic site, suggest that different Ubcs may utilize catalytic mechanisms of varying, efficiency and substrate specificity.
+<StructureSection load='1u9b' size='340' side='right'caption='[[1u9b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1u9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U9B 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&#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=1u9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9b OCA], [https://pdbe.org/1u9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9b RCSB], [https://www.ebi.ac.uk/pdbsum/1u9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9b ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 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. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</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/u9/1u9b_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=1u9b ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for the viability of yeast cells with a specific role in the G2-M transition of the cell cycle. The structure of recombinant mammalian Ubc9 has been determined from two crystal forms at 2.0 A resolution. Like Arabidopsis thaliana Ubc1 and S. cerevisiae Ubc4, murine/human Ubc9 was crystallized as a monomer, suggesting that previously reported hetero- and homo-interactions among Ubcs may be relatively weak or indirect. Compared with the known crystal structures of Ubc1 and Ubc4, which regulate different cellular processes, Ubc9 has a 5-residue insertion that forms a very exposed tight beta-hairpin and a 2-residue insertion that forms a bulge in a loop close to the active site. Mammalian Ubc9 also possesses a distinct electrostatic potential distribution that may provide possible clues to its remarkable ability to interact with other proteins. The 2-residue insertion and other sequence and structural heterogeneity observed at the catalytic site suggest that different Ubcs may utilize catalytic mechanisms of varying efficiency and substrate specificity.
-==About this Structure==
+Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system.,Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK J Biol Chem. 1997 Aug 22;272(34):21381-7. PMID:9261152<ref>PMID:9261152</ref>
-U9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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: C93. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U9B OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system., Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK, J Biol Chem. 1997 Aug 22;272(34):21381-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9261152 9261152]
+</div>
+<div class="pdbe-citations 1u9b" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Bernards R]]
-[[Category: Ubiquitin--protein ligase]]
+[[Category: Hateboer G]]
-[[Category: Bernards, R.]]
+[[Category: Perrakis A]]
-[[Category: Hateboer, G.]]
+[[Category: Sixma TK]]
-[[Category: Perrakis, A.]]
+[[Category: Tong H]]
-[[Category: Sixma, T.K.]]
-[[Category: Tong, H.]]
-[[Category: cell cycle control]]
-[[Category: ligase]]
-[[Category: ubiquitin-conjugating enzyme]]
-[[Category: ubiquitin-directed proteolysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 17:06:22 2007''