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2iy1

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(New page: 200px<br /> <applet load="2iy1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iy1, resolution 2.46&Aring;" /> '''SENP1 (MUTANT) FULL...)
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[[Image:2iy1.gif|left|200px]]<br />
 
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<applet load="2iy1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2iy1, resolution 2.46&Aring;" />
 
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'''SENP1 (MUTANT) FULL LENGTH SUMO1'''<br />
 
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==Overview==
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==SENP1 (mutant) full length SUMO1==
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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.
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<StructureSection load='2iy1' size='340' side='right'caption='[[2iy1]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iy1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Disease==
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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>
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Known diseases associated with this structure: Orofacial cleft 10 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601912 601912]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2IY1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IY1 OCA].
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</div>
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<div class="pdbe-citations 2iy1" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17099698 17099698]
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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*[[Sentrin-specific protease|Sentrin-specific protease]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Dong, C.]]
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[[Category: Dong C]]
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[[Category: Naismith, J.H.]]
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[[Category: Naismith JH]]
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[[Category: Shen, L.]]
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[[Category: Shen L]]
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[[Category: hydrolase]]
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[[Category: hydrolase/nuclear protein complex]]
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[[Category: nuclear protein]]
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[[Category: protease]]
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[[Category: protein protein complex]]
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[[Category: thiol protease]]
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[[Category: ubiquitin]]
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[[Category: ubl conjugation pathway]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:49:33 2007''
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Current revision

SENP1 (mutant) full length SUMO1

PDB ID 2iy1

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