1euv

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[[Image:1euv.gif|left|200px]]
 
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{{Structure
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==X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.==
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|PDB= 1euv |SIZE=350|CAPTION= <scene name='initialview01'>1euv</scene>, resolution 1.6&Aring;
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<StructureSection load='1euv' size='340' side='right'caption='[[1euv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1euv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUV FirstGlance]. <br>
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|ACTIVITY=
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</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=1euv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euv OCA], [https://pdbe.org/1euv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1euv RCSB], [https://www.ebi.ac.uk/pdbsum/1euv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1euv ProSAT]</span></td></tr>
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|GENE=
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</table>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/ULP1_YEAST ULP1_YEAST] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.<ref>PMID:10094048</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/eu/1euv_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=1euv 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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Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.
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'''X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.'''
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Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.,Mossessova E, Lima CD Mol Cell. 2000 May;5(5):865-76. PMID:10882122<ref>PMID:10882122</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1euv" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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== References ==
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==About this Structure==
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<references/>
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1EUV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUV OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast., Mossessova E, Lima CD, Mol Cell. 2000 May;5(5):865-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10882122 10882122]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Lima, C D.]]
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[[Category: Lima CD]]
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[[Category: Mossessova, E.]]
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[[Category: Mossessova E]]
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[[Category: covalent protease adduct]]
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[[Category: cysteine protease]]
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[[Category: nabh4]]
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[[Category: smt3 hydrolase desumoylating enzyme]]
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[[Category: smt3 processing enzyme]]
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[[Category: sumo hydrolase]]
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[[Category: sumo processing enzyme]]
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[[Category: thiohemiacetal]]
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[[Category: ubiquitin-like protease 1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:35 2008''
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Current revision

X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.

PDB ID 1euv

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