2iy1: Difference between revisions

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-{{Seed}}
-[[Image:2iy1.png|left|200px]]
-<!--
+==SENP1 (mutant) full length SUMO1==
-The line below this paragraph, containing "STRUCTURE_2iy1", creates the "Structure Box" on the page.
+<StructureSection load='2iy1' size='340' side='right'caption='[[2iy1]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2iy1]] is a 4 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=2IY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY1 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.46&#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=2iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy1 OCA], [https://pdbe.org/2iy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy1 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy1 ProSAT]</span></td></tr>
-{{STRUCTURE_2iy1|  PDB=2iy1  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</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/iy/2iy1_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=2iy1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from modified proteins. To establish the proteolytic mechanism, we determined structures of catalytically inactive SENP1 bound to SUMO-1-modified RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond is kinked at a right angle to the C-terminal tail of SUMO-1 and has the cis configuration of the amide nitrogens. SENP1 preferentially processes SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.
-===SENP1 (MUTANT) FULL LENGTH SUMO1===
+SUMO protease SENP1 induces isomerization of the scissile peptide bond.,Shen L, Tatham MH, Dong C, Zagorska A, Naismith JH, Hay RT Nat Struct Mol Biol. 2006 Dec;13(12):1069-77. Epub 2006 Nov 12. PMID:17099698<ref>PMID:17099698</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iy1" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17099698}}, adds the Publication Abstract to the page
+*[[SUMO 3D Structures|SUMO 3D Structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17099698 is the PubMed ID number.
+*[[Sentrin-specific protease|Sentrin-specific protease]]
--->
+== References ==
-{{ABSTRACT_PUBMED_17099698}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-IY1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY1 OCA].
-==Reference==
-SUMO protease SENP1 induces isomerization of the scissile peptide bond., Shen L, Tatham MH, Dong C, Zagorska A, Naismith JH, Hay RT, Nat Struct Mol Biol. 2006 Dec;13(12):1069-77. Epub 2006 Nov 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17099698 17099698]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Dong, C.]]
+[[Category: Dong C]]
-[[Category: Naismith, J H.]]
+[[Category: Naismith JH]]
-[[Category: Shen, L.]]
+[[Category: Shen L]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase/nuclear protein complex]]
-[[Category: Nuclear protein]]
-[[Category: Protease]]
-[[Category: Protein protein complex]]
-[[Category: Thiol protease]]
-[[Category: Ubiquitin]]
-[[Category: Ubl conjugation pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:44:54 2008''