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==Solution structure of At5g66040, a putative protein from Arabidosis Thaliana== | |||
<StructureSection load='1tq1' size='340' side='right'caption='[[1tq1]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TQ1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1tq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tq1 OCA], [https://pdbe.org/1tq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1tq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tq1 ProSAT], [https://www.topsan.org/Proteins/CESG/1tq1 TOPSAN]</span></td></tr> | |||
</table> | |||
| | == Function == | ||
[https://www.uniprot.org/uniprot/STR16_ARATH STR16_ARATH] Thought to act during the early stages of leaf senescence. Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is thiosulfate > 3-mercaptopyruvate.<ref>PMID:12482606</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/tq/1tq1_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=1tq1 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We describe the three-dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single-domain sulfurtransferase and is annotated as a senescence-associated protein (sen1-like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily/STR_genefamily.html). The sequence of At5g66040.1 is virtually identical to that of a protein from Arabidopsis found by others to confer ketoconazole resistance in yeast. Comparison of the three-dimensional structure with those in the Protein Data Bank revealed that At5g66040.1 contains an additional mobile beta-hairpin not found in other rhodaneses that may function in binding specific substrates. This represents the first structure of a single-domain plant sulfurtransferase. The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins. Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases. | We describe the three-dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single-domain sulfurtransferase and is annotated as a senescence-associated protein (sen1-like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily/STR_genefamily.html). The sequence of At5g66040.1 is virtually identical to that of a protein from Arabidopsis found by others to confer ketoconazole resistance in yeast. Comparison of the three-dimensional structure with those in the Protein Data Bank revealed that At5g66040.1 contains an additional mobile beta-hairpin not found in other rhodaneses that may function in binding specific substrates. This represents the first structure of a single-domain plant sulfurtransferase. The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins. Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases. | ||
Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana.,Cornilescu G, Vinarov DA, Tyler EM, Markley JL, Cornilescu CC Protein Sci. 2006 Dec;15(12):2836-41. Epub 2006 Nov 6. PMID:17088324<ref>PMID:17088324</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1tq1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cornilescu CC]] | |||
[[Category: Cornilescu | [[Category: Cornilescu G]] | ||
[[Category: Cornilescu | [[Category: Lee MS]] | ||
[[Category: Lee | [[Category: Markley JL]] | ||
[[Category: Markley | [[Category: Shahan MN]] | ||
[[Category: Shahan | [[Category: Singh S]] | ||
[[Category: Singh | [[Category: Tyler EM]] | ||
[[Category: Tyler | [[Category: Vinarov D]] | ||
[[Category: Vinarov | |||
Latest revision as of 12:13, 22 May 2024
Solution structure of At5g66040, a putative protein from Arabidosis ThalianaSolution structure of At5g66040, a putative protein from Arabidosis Thaliana
Structural highlights
FunctionSTR16_ARATH Thought to act during the early stages of leaf senescence. Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is thiosulfate > 3-mercaptopyruvate.[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 PubMedWe describe the three-dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single-domain sulfurtransferase and is annotated as a senescence-associated protein (sen1-like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily/STR_genefamily.html). The sequence of At5g66040.1 is virtually identical to that of a protein from Arabidopsis found by others to confer ketoconazole resistance in yeast. Comparison of the three-dimensional structure with those in the Protein Data Bank revealed that At5g66040.1 contains an additional mobile beta-hairpin not found in other rhodaneses that may function in binding specific substrates. This represents the first structure of a single-domain plant sulfurtransferase. The enzymatically active cysteine-containing domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases, and stress proteins such as senescence specific protein 1 in plants, PspE and GlpE in bacteria, and cyanide and arsenate resistance proteins. Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases. Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana.,Cornilescu G, Vinarov DA, Tyler EM, Markley JL, Cornilescu CC Protein Sci. 2006 Dec;15(12):2836-41. Epub 2006 Nov 6. PMID:17088324[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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