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1euv

From Proteopedia

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

Structural highlights

1euv is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li SJ, Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 1999 Mar 18;398(6724):246-51. PMID:10094048 doi:http://dx.doi.org/10.1038/18457
↑ Mossessova E, Lima CD. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol Cell. 2000 May;5(5):865-76. PMID:10882122

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1euv"

Categories: Large Structures | Saccharomyces cerevisiae | Lima CD | Mossessova E

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1euv.png|left|200px]]
-<!--
+==X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.==
-The line below this paragraph, containing "STRUCTURE_1euv", creates the "Structure Box" on the page.
+<StructureSection load='1euv' size='340' side='right'caption='[[1euv]], [[Resolution|resolution]] 1.60&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'>[[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>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+</table>
-{{STRUCTURE_1euv|  PDB=1euv  |  SCENE=  }}
+== Function ==
+[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>
+== 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/eu/1euv_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=1euv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1euv" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10882122}}, adds the Publication Abstract to the page
+*[[SUMO 3D Structures|SUMO 3D Structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10882122 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10882122}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-EUV is a 2 chains 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].
-==Reference==
-<ref group="xtra">PMID:10882122</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Lima, C D.]]
+[[Category: Lima CD]]
-[[Category: Mossessova, E.]]
+[[Category: Mossessova E]]
-[[Category: Covalent protease adduct]]
-[[Category: Cysteine protease]]
-[[Category: Nabh4]]
-[[Category: Smt3 hydrolase desumoylating enzyme]]
-[[Category: Smt3 processing enzyme]]
-[[Category: Sumo hydrolase]]
-[[Category: Sumo processing enzyme]]
-[[Category: Thiohemiacetal]]
-[[Category: Ubiquitin-like protease 1]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:37:02 2009''

1euv

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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