5b52: Difference between revisions

Line 1:

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

~~The entry~~ 5b52 is ~~ON HOLD until Paper~~ Publication

==Crystal structure of the N-terminal domain of H-NS family protein TurB==

== Structural highlights ==

<table><tr><td colspan='2'>[[5b52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B52 FirstGlance]. <br>

</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=5b52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b52 OCA], [http://pdbe.org/5b52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b52 RCSB], [http://www.ebi.ac.uk/pdbsum/5b52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b52 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.

~~Authors:~~ Suzuki-Minakuchi, C., Nojiri, H.

Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440.,Suzuki-Minakuchi C, Kawazuma K, Matsuzawa J, Vasileva D, Fujimoto Z, Terada T, Okada K, Nojiri H FEBS Lett. 2016 Oct 6. doi: 10.1002/1873-3468.12425. PMID:27709616<ref>PMID:27709616</ref>

~~Description: Crystal structure~~ of the N-~~terminal domain of H~~-~~NS family protein TurB~~

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

~~[[Category: Unreleased Structures]]~~

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Nojiri, H]]

[[Category: Suzuki-Minakuchi, C]]

[[Category: Nucleoid associated protein]]

[[Category: Transcription]]

[[Category: Transcriptional regulator]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5b52 is ON HOLD  until Paper Publication
+==Crystal structure of the N-terminal domain of H-NS family protein TurB==
+<StructureSection load='5b52' size='340' side='right' caption='[[5b52]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5b52]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B52 FirstGlance]. <br>
+</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=5b52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b52 OCA], [http://pdbe.org/5b52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b52 RCSB], [http://www.ebi.ac.uk/pdbsum/5b52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b52 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.
-Authors: Suzuki-Minakuchi, C., Nojiri, H.
+Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440.,Suzuki-Minakuchi C, Kawazuma K, Matsuzawa J, Vasileva D, Fujimoto Z, Terada T, Okada K, Nojiri H FEBS Lett. 2016 Oct 6. doi: 10.1002/1873-3468.12425. PMID:27709616<ref>PMID:27709616</ref>
-Description: Crystal structure of the N-terminal domain of H-NS family protein TurB
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5b52" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Nojiri, H]]
 [[Category: Suzuki-Minakuchi, C]]
+[[Category: Nucleoid associated protein]]
+[[Category: Transcription]]
+[[Category: Transcriptional regulator]]