3wrw
From Proteopedia
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| - | ''' | + | ==Crystal structure of the N-terminal domain of resistance protein== |
| + | <StructureSection load='3wrw' size='340' side='right' caption='[[3wrw]], [[Resolution|resolution]] 2.71Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wrw]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRW FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vkw|3vkw]], [[3wrv|3wrv]], [[3wrx|3wrx]], [[3wry|3wry]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wrw RCSB], [http://www.ebi.ac.uk/pdbsum/3wrw PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tm-1, the protein product of Tm-1, a semidominant resistance gene of tomato, inhibits tomato mosaic virus (ToMV) replication by binding to ToMV replication proteins. Previous studies suggested the importance of the Tm-1 N-terminal region for its inhibitory activity; however, it has not been determined if the N-terminal region is sufficient for inhibition. Furthermore, the three-dimensional structure of Tm-1 has not been determined. In this study, an N-terminal fragment of Tm-1 (residues 1-431) as a fusion protein containing an upstream maltose-binding protein was expressed in E. coli Rosetta (DE3) cells at 30 degrees C and then purified. The solubility of the fusion protein was greater when the cells were cultured at 30 degrees C than when cultured at lower or higher temperatures. The purified N-terminal Tm-1 fragment from which the maltose-binding protein tag had been removed has inhibitory activity against ToMV RNA replication. | ||
| - | + | Expression, purification, and functional characterization of an N-terminal fragment of the tomato mosaic virus resistance protein Tm-1.,Kato M, Ishibashi K, Kobayashi C, Ishikawa M, Katoh E Protein Expr Purif. 2013 May;89(1):1-6. doi: 10.1016/j.pep.2013.02.001. Epub 2013, Feb 13. PMID:23415925<ref>PMID:23415925</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Katoh, E.]] | ||
| + | [[Category: Kezuka, Y.]] | ||
| + | [[Category: Alpha/beta domain]] | ||
| + | [[Category: Resistance factor]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 09:00, 13 August 2014
Crystal structure of the N-terminal domain of resistance protein
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