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==Crystal structure of NN domain of resistance protein==
==Crystal structure of NN domain of resistance protein==
<StructureSection load='3wrv' size='340' side='right' caption='[[3wrv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='3wrv' size='340' side='right' caption='[[3wrv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<table><tr><td colspan='2'>[[3wrv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRV FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wrv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRV FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vkw|3vkw]], [[3wrw|3wrw]], [[3wrx|3wrx]], [[3wry|3wry]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vkw|3vkw]], [[3wrw|3wrw]], [[3wrx|3wrx]], [[3wry|3wry]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wrv RCSB], [http://www.ebi.ac.uk/pdbsum/3wrv PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrv OCA], [http://pdbe.org/3wrv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wrv RCSB], [http://www.ebi.ac.uk/pdbsum/3wrv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrv ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== 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.
Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of Tm-1 are reported. A three-wavelength MAD data set was collected from a selenomethionine-labelled crystal and processed to 2.7 A resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 A, alpha = 94.6, beta = 109.3, gamma = 108.0 degrees .


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>
Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.,Kato M, Kezuka Y, Kobayashi C, Ishibashi K, Nonaka T, Ishikawa M, Katoh E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1411-4. doi:, 10.1107/S1744309113030819. Epub 2013 Nov 29. PMID:24316842<ref>PMID:24316842</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
<div class="pdbe-citations 3wrv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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