5xw7: Difference between revisions

Line 1:

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

~~The entry~~ 5xw7 is ~~ON HOLD until Paper~~ Publication

==Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthase subunit C==

== Structural highlights ==

<table><tr><td colspan='2'>[[5xw7]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW7 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=5xw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw7 OCA], [http://pdbe.org/5xw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw7 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a beta-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra alpha-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted alpha-helix. Such structural feature indicates that the inserted alpha-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the alpha-helical hinge may play important role for exporting glucan chains.

~~Authors~~:

Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.,Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M Sci Rep. 2017 Oct 12;7(1):13018. doi: 10.1038/s41598-017-12530-0. PMID:29026093<ref>PMID:29026093</ref>

~~Description~~:

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

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

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Kato, K]]

[[Category: Nojima, S]]

[[Category: Yao, M]]

[[Category: Biosynthetic protein]]

[[Category: Cellulose synthase]]

[[Category: Tetratrico peptide repeat]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5xw7 is ON HOLD  until Paper Publication
+==Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthase subunit C==
+<StructureSection load='5xw7' size='340' side='right' caption='[[5xw7]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5xw7]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW7 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=5xw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw7 OCA], [http://pdbe.org/5xw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw7 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a beta-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra alpha-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted alpha-helix. Such structural feature indicates that the inserted alpha-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the alpha-helical hinge may play important role for exporting glucan chains.
-Authors:
+Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.,Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M Sci Rep. 2017 Oct 12;7(1):13018. doi: 10.1038/s41598-017-12530-0. PMID:29026093<ref>PMID:29026093</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5xw7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Kato, K]]
+[[Category: Nojima, S]]
+[[Category: Yao, M]]
+[[Category: Biosynthetic protein]]
+[[Category: Cellulose synthase]]
+[[Category: Tetratrico peptide repeat]]