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1gps
From Proteopedia
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==SOLUTION STRUCTURE OF GAMMA 1-H AND GAMMA 1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY 1H-NMR: A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS== | ==SOLUTION STRUCTURE OF GAMMA 1-H AND GAMMA 1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY 1H-NMR: A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS== | ||
| - | <StructureSection load='1gps' size='340' side='right' caption='[[1gps | + | <StructureSection load='1gps' size='340' side='right'caption='[[1gps]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1gps]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1gps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_turgidum Triticum turgidum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPS FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=1gps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gps OCA], [https://pdbe.org/1gps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gps RCSB], [https://www.ebi.ac.uk/pdbsum/1gps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gps ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DEF1_WHEAT DEF1_WHEAT] Inhibits protein translation in cell-free systems. |
== 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/gp/1gps_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gps_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> | ||
| Line 18: | Line 19: | ||
</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=1gps ConSurf]. | </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=1gps ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The complete assignment of the proton NMR spectra of the homologous gamma 1-hordothionin and gamma 1-purothionin (47 amino acids, 4 disulfide bridges) from barley and wheat, respectively, has been performed by two-dimensional sequence-specific methods. A total of 299 proton-proton distance constraints for gamma 1-H and 285 for gamma 1-P derived from NOESY spectra have been used to calculate the three-dimensional solution structures. Initial structures have been generated by distance geometry methods and further refined by dynamical simulated annealing calculations. Both proteins show identical secondary and tertiary structure with a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. Moreover, a clustering of positive charges is observed on the face of the beta-sheet opposite to the helix. The three-dimensional structures of the gamma-thionins differ remarkably from plant alpha- and beta-thionins and crambin. However, they show a higher structural analogy with scorpion toxins and insect defensins which also present the CSH motif. | ||
| - | + | ==See Also== | |
| - | + | *[[Plant defensin|Plant defensin]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bruix | + | [[Category: Triticum turgidum]] |
| - | [[Category: Colilla | + | [[Category: Bruix M]] |
| - | [[Category: Gonzalez | + | [[Category: Colilla FJ]] |
| - | [[Category: Jimenez | + | [[Category: Gonzalez C]] |
| - | [[Category: Mendez | + | [[Category: Jimenez MA]] |
| - | [[Category: Rico | + | [[Category: Mendez E]] |
| - | [[Category: Santoro | + | [[Category: Rico M]] |
| - | + | [[Category: Santoro J]] | |
Current revision
SOLUTION STRUCTURE OF GAMMA 1-H AND GAMMA 1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY 1H-NMR: A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS
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Categories: Large Structures | Triticum turgidum | Bruix M | Colilla FJ | Gonzalez C | Jimenez MA | Mendez E | Rico M | Santoro J
