1rhs

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(New page: 200px<br /><applet load="1rhs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhs, resolution 1.36&Aring;" /> '''SULFUR-SUBSTITUTED R...)
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[[Image:1rhs.jpg|left|200px]]<br /><applet load="1rhs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rhs, resolution 1.36&Aring;" />
 
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'''SULFUR-SUBSTITUTED RHODANESE'''<br />
 
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==Overview==
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==SULFUR-SUBSTITUTED RHODANESE==
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In the course of the reaction catalyzed by rhodanese, the enzyme cycles, between two catalytic intermediates, the sulfur-free and the, sulfur-substituted (persulfide-containing) forms. The crystal structure of, sulfur-free rhodanese, which was prepared in solution and then, crystallized, is highly similar to that of sulfur-substituted enzyme. The, inactivation of sulfur-free rhodanese with a small molar excess of, hydrogen peroxide relies essentially on a modification limited to the, active site, consisting of the oxidation of the essential sulfhydryl to, sulfenyl group (-S-OH). Upon reaction of the sulfur-free enzyme with, monoiodoacetate in the crystal, the Cys-247 side chain with the bound, carboxymethyl group is forced into a conformation that allows favorable, interactions of the carboxylate with the four peptide NH groups that, participate in hydrogen bonding interactions with the transferable sulfur, atom of the persulfide group in the sulfur-substituted rhodanese. It is, concluded that active site-specific chemical modifications of sulfur-free, rhodanese do not lead to significant changes of the protein structure, consistent with a high degree of similarity of the structures of the, sulfur-free and sulfur-substituted forms of the enzyme both in solution, and in the crystal.
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<StructureSection load='1rhs' size='340' side='right'caption='[[1rhs]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rhs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RHS 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]] 1.36&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></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=1rhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhs OCA], [https://pdbe.org/1rhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rhs RCSB], [https://www.ebi.ac.uk/pdbsum/1rhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THTR_BOVIN THTR_BOVIN] Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur.
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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/rh/1rhs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rhs 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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1.36 A resolution X-ray diffraction data have been recorded at 100 K for bovine liver sulfur-substituted rhodanese, using synchrotron radiation. The crystal structure has been refined anisotropically to a final R factor of 0.159 (Rfree = 0.229) for 53034 unique reflections. The model contains 2327 protein atoms and 407 solvent molecules, with a good geometry. The high resolution allows full details for helices, beta-sheets, tight turns and of all inter- and intramolecular interactions stabilizing the enzyme molecule to be given. The situation at the active site is described, particularly in regard to the network of hydrogen bonds made by Sgamma and Sdelta of the sulfur-substituted catalytic Cys247 and surrounding groups and solvent molecules. The replacement of the precipitant ammonium sulfate with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site. Only limited changes of the enzyme structure have been found as a result of the drastic change in the crystal medium.
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==About this Structure==
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Structure of sulfur-substituted rhodanese at 1.36 A resolution.,Gliubich F, Berni R, Colapietro M, Barba L, Zanotti G Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):481-6. PMID:9761843<ref>PMID:9761843</ref>
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1RHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RHS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Active site structural features for chemically modified forms of rhodanese., Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R, J Biol Chem. 1996 Aug 30;271(35):21054-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8702871 8702871]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1rhs" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thiosulfate sulfurtransferase]]
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[[Category: Barba, L.]]
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[[Category: Colapietro, M.]]
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[[Category: Gliubich, F.]]
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[[Category: Zanotti, G.]]
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[[Category: rhodanese]]
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[[Category: sulfurtransferase]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:36:26 2007''
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==See Also==
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*[[Sulfurtransferase|Sulfurtransferase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Barba L]]
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[[Category: Colapietro M]]
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[[Category: Gliubich F]]
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[[Category: Zanotti G]]

Current revision

SULFUR-SUBSTITUTED RHODANESE

PDB ID 1rhs

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