1urh: Difference between revisions

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-{{Seed}}
-[[Image:1urh.png|left|200px]]
-<!--
+==The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli==
-The line below this paragraph, containing "STRUCTURE_1urh", creates the "Structure Box" on the page.
+<StructureSection load='1urh' size='340' side='right'caption='[[1urh]], [[Resolution|resolution]] 2.80&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'>[[1urh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URH 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]] 2.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene></td></tr>
-{{STRUCTURE_1urh|  PDB=1urh  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1urh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1urh OCA], [https://pdbe.org/1urh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1urh RCSB], [https://www.ebi.ac.uk/pdbsum/1urh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1urh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/THTM_ECOLI THTM_ECOLI] Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity.
+== 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/ur/1urh_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1urh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+-Mercaptopyruvate sulfurtransferases (MSTs) catalyze, in vitro, the transfer of a sulfur atom from substrate to cyanide, yielding pyruvate and thiocyanate as products. They display clear structural homology with the protein fold observed in the rhodanese sulfurtransferase family, composed of two structurally related domains. The role of MSTs in vivo, as well as their detailed molecular mechanisms of action have been little investigated. Here, we report the crystal structure of SseA, a MST from Escherichia coli, which is the first MST three-dimensional structure disclosed to date. SseA displays specific structural differences relative to eukaryotic and prokaryotic rhodaneses. In particular, conformational variation of the rhodanese active site loop, hosting the family invariant catalytic Cys residue, may support a new sulfur transfer mechanism involving Cys237 as the nucleophilic species and His66, Arg102 and Asp262 as residues assisting catalysis.
-===THE "RHODANESE" FOLD AND CATALYTIC MECHANISM OF 3-MERCAPTOPYRUVATE SULFOTRANSFERASES: CRYSTAL STRUCTURE OF SSEA FROM ESCHERICHIA COLI===
+The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli.,Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D J Mol Biol. 2004 Jan 9;335(2):583-93. PMID:14672665<ref>PMID:14672665</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1urh" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14672665}}, adds the Publication Abstract to the page
+*[[Sulfurtransferase|Sulfurtransferase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14672665 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14672665}}
+__TOC__
+</StructureSection>
-==About this Structure==
-URH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URH OCA].
-==Reference==
-<ref group="xtra">PMID:14672665</ref><references group="xtra"/>
-[[Category: 3-mercaptopyruvate sulfurtransferase]]
 [[Category: Escherichia coli]]
-[[Category: Armirotti, A.]]
+[[Category: Large Structures]]
-[[Category: Bolognesi, M.]]
+[[Category: Armirotti A]]
-[[Category: Bordo, D.]]
+[[Category: Bolognesi M]]
-[[Category: Carpen, A.]]
+[[Category: Bordo D]]
-[[Category: Forlani, F.]]
+[[Category: Carpen A]]
-[[Category: Pagani, S.]]
+[[Category: Forlani F]]
-[[Category: Spallarossa, A.]]
+[[Category: Pagani S]]
-[[Category: Rhodanese]]
+[[Category: Spallarossa A]]
-[[Category: Sulfur-transferase]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:58:58 2009''