1vee: Difference between revisions
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==NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana== | ==NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana== | ||
<StructureSection load='1vee' size='340' side='right' caption='[[1vee | <StructureSection load='1vee' size='340' side='right'caption='[[1vee]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vee]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1vee]] 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=1VEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VEE FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vee OCA], [https://pdbe.org/1vee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vee RCSB], [https://www.ebi.ac.uk/pdbsum/1vee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vee ProSAT], [https://www.topsan.org/Proteins/RSGI/1vee TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/STR4_ARATH STR4_ARATH] Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).<ref>PMID:19682289</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1vee_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1vee_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1vee ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Line 31: | Line 32: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Guntert | [[Category: Large Structures]] | ||
[[Category: Inoue | [[Category: Guntert P]] | ||
[[Category: Kigawa | [[Category: Inoue M]] | ||
[[Category: Koshiba | [[Category: Kigawa T]] | ||
[[Category: Lopez-Mendez | [[Category: Koshiba S]] | ||
[[Category: Pantoja-Uceda | [[Category: Lopez-Mendez B]] | ||
[[Category: Pantoja-Uceda D]] | |||
[[Category: Seki | [[Category: Seki M]] | ||
[[Category: Shinozaki | [[Category: Shinozaki K]] | ||
[[Category: Shirouzu | [[Category: Shirouzu M]] | ||
[[Category: Tanaka | [[Category: Tanaka A]] | ||
[[Category: Terada | [[Category: Terada T]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 03:02, 28 December 2023
NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thalianaNMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana
Structural highlights
FunctionSTR4_ARATH Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).[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 PubMedThe three-dimensional structure of the rhodanese homology domain At4g01050(175-195) from Arabidopsis thaliana has been determined by solution nuclear magnetic resonance methods based on 3043 upper distance limits derived from NOE intensities measured in three-dimensional NOESY spectra. The structure shows a backbone root mean square deviation to the mean coordinates of 0.43 A for the structured residues 7-125. The fold consists of a central parallel beta-sheet with five strands in the order 1-5-4-2-3 and arranged in the conventional counterclockwise twist, and helices packing against each side of the beta-sheet. Comparison with the sequences of other proteins with a rhodanese homology domain in Arabidopsis thaliana indicated residues that could play an important role in the scaffold of the rhodanese homology domain. Finally, a three-dimensional structure comparison of the present noncatalytic rhodanese homology domain with the noncatalytic rhodanese domains of sulfurtransferases from other organisms discloses differences in the length and conformation of loops that could throw light on the role of the noncatalytic rhodanese domain in sulfurtransferases. Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana.,Pantoja-Uceda D, Lopez-Mendez B, Koshiba S, Inoue M, Kigawa T, Terada T, Shirouzu M, Tanaka A, Seki M, Shinozaki K, Yokoyama S, Guntert P Protein Sci. 2005 Jan;14(1):224-30. Epub 2004 Dec 2. PMID:15576557[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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