3wrv: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal structure of NN domain of resistance protein==

== Structural highlights ==

<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>

<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=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>

<table>

== 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.

~~The entry 3wrv is ON HOLD~~

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>

~~Authors: Matsumura~~, H., Katoh, E.

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

</div>

~~Description~~: ~~Crystal structure of NN~~ domain ~~of resistance protein~~

== References ==

__TOC__

</StructureSection>

[[Category: Katoh, E.]]

[[Category: Matsumura, H.]]

[[Category: Alpha/beta domain]]

[[Category: Resistance]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of NN domain of resistance protein==
+<StructureSection load='3wrv' size='340' side='right' caption='[[3wrv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
+== Structural highlights ==
+<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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vkw|3vkw]], [[3wrw|3wrw]], [[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=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>
+<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.
-The entry 3wrv is ON HOLD
+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>
-Authors: Matsumura, H., Katoh, E.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of NN domain of resistance protein
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Katoh, E.]]
+[[Category: Matsumura, H.]]
+[[Category: Alpha/beta domain]]
+[[Category: Resistance]]
+[[Category: Transferase]]