1h4m

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[[Image:1h4m.gif|left|200px]]<br /><applet load="1h4m" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h4m, resolution 2.1&Aring;" />
 
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'''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE'''<br />
 
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==Overview==
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==Sulfurtransferase from Azotobacter vinelandii in complex with phosphate==
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<StructureSection load='1h4m' size='340' side='right'caption='[[1h4m]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h4m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4M 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]] 2.1&#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=EDO:1,2-ETHANEDIOL'>EDO</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=1h4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4m OCA], [https://pdbe.org/1h4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4m RCSB], [https://www.ebi.ac.uk/pdbsum/1h4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THTR_AZOVI THTR_AZOVI]
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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/h4/1h4m_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=1h4m 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 ==
Active site reactivity and specificity of RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been investigated through ligand binding, site-directed mutagenesis, and X-ray crystallographic techniques, in a combined approach. In native RhdA the active site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity measurements show that phosphate anions interact with Cys230 persulfide sulfur atom and modulate activity. Crystallographic analyses confirm that phosphate and hypophosphite anions react with native RhdA, removing the persulfide sulfur atom from the active site pocket. Considering that RhdA and the catalytic subunit of Cdc25 phosphatases share a common three-dimensional fold as well as active site Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid insertion at the active site loop were designed and their phosphatase activity tested. The crystallographic and functional results reported here show that specific sulfurtransferase or phosphatase activities are strictly related to precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase, respectively.
Active site reactivity and specificity of RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been investigated through ligand binding, site-directed mutagenesis, and X-ray crystallographic techniques, in a combined approach. In native RhdA the active site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity measurements show that phosphate anions interact with Cys230 persulfide sulfur atom and modulate activity. Crystallographic analyses confirm that phosphate and hypophosphite anions react with native RhdA, removing the persulfide sulfur atom from the active site pocket. Considering that RhdA and the catalytic subunit of Cdc25 phosphatases share a common three-dimensional fold as well as active site Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid insertion at the active site loop were designed and their phosphatase activity tested. The crystallographic and functional results reported here show that specific sulfurtransferase or phosphatase activities are strictly related to precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase, respectively.
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==About this Structure==
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A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese.,Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S Biol Chem. 2001 Aug;382(8):1245-52. PMID:11592406<ref>PMID:11592406</ref>
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1H4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4M 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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A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese., Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S, Biol Chem. 2001 Aug;382(8):1245-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11592406 11592406]
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</div>
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[[Category: Azotobacter vinelandii]]
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<div class="pdbe-citations 1h4m" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thiosulfate sulfurtransferase]]
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[[Category: Bolognesi, M.]]
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[[Category: Bordo, D.]]
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[[Category: Carpen, A.]]
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[[Category: Colnaghi, R.]]
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[[Category: Forlani, F.]]
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[[Category: Pagani, S.]]
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[[Category: Spallarossa, A.]]
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[[Category: EDO]]
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[[Category: sulfur metabolism]]
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[[Category: sulfurtransferase]]
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[[Category: thiosulfate:cyanide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:20 2008''
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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: Azotobacter vinelandii]]
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[[Category: Large Structures]]
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[[Category: Bolognesi M]]
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[[Category: Bordo D]]
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[[Category: Carpen A]]
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[[Category: Colnaghi R]]
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[[Category: Forlani F]]
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[[Category: Pagani S]]
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[[Category: Spallarossa A]]

Current revision

Sulfurtransferase from Azotobacter vinelandii in complex with phosphate

PDB ID 1h4m

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