1gpt

<StructureSection load='1gpt' size='340' side='right'caption='[[1gpt]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1gpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Barley Barley]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPT FirstGlance]. <br>

</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=1gpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpt OCA], [https://pdbe.org/1gpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpt RCSB], [https://www.ebi.ac.uk/pdbsum/1gpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpt ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/DEF1_HORVU DEF1_HORVU]] Inhibits protein translation in cell-free systems.

<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.

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.,Bruix M, Jimenez MA, Santoro J, Gonzalez C, Colilla FJ, Mendez E, Rico M Biochemistry. 1993 Jan 19;32(2):715-24. PMID:8380707<ref>PMID:8380707</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1gpt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Barley]]

[[Category: Bruix, M]]

[[Category: Colilla, F J]]

[[Category: Gonzalez, C]]

[[Category: Jimenez, M A]]

[[Category: Mendez, E]]

[[Category: Rico, M]]

[[Category: Santoro, J]]

[[Category: Plant toxin]]