6q5m: Difference between revisions

Line 1:

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

~~The entry~~ 6q5m is ~~ON HOLD until Paper~~ Publication

==Crystal structure of a CC-Hex mutant that forms an antiparallel four-helix coiled coil CC-Hex*-L24Dab==

== Structural highlights ==

<table><tr><td colspan='2'>[[6q5m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q5M FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DAB:2,4-DIAMINOBUTYRIC+ACID'>DAB</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6q5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q5m OCA], [http://pdbe.org/6q5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q5m RCSB], [http://www.ebi.ac.uk/pdbsum/6q5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q5m ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

The association of amphipathic alpha helices in water leads to alpha-helical-bundle protein structures. However, the driving force for this-the hydrophobic effect-is not specific and does not define the number or the orientation of helices in the associated state. Rather, this is achieved through deeper sequence-to-structure relationships, which are increas-ingly being discerned. For example, for one structurally extreme but nevertheless ubiquitous class of bundle-the alpha-helical coiled coils-relationships have been established that discriminate between all-parallel dimers, trimers and tetramers. Association states above this are known, as are antiparallel and mixed arrangements of the helices. However, these alternative states are less-well understood. Here, we describe a synthetic-peptide system that switches be-tween parallel hexamers and various up-down-up-down tetramers in response to single-amino-acid changes and solution conditions. The main accessible states of each peptide variant are characterized fully in solution and, in most cases, to high resolution with X-ray crystal structures. Analysis and inspection of these structures helps rationalize the different states formed. This navigation of the structural landscape of alpha-helical coiled coils above the dimers and tri-mers that dominate in nature has allowed us to design rationally a well-defined and hyperstable antiparallel coiled-coil tetramer (apCC-Tet). This robust de novo protein provides another scaffold for further structural and functional designs in protein engineering and synthetic biology.

~~Authors:~~ Wood~~, C.W.~~, Beesley, ~~J.L.~~, ~~Rhys~~, ~~G.G.~~, ~~Brady~~, R.L.~~, Woolfson, D~~.N.

Navigating the structural landscape of de novo alpha-helical bundles.,Rhys GG, Wood CW, Beesley JL, Zaccai NR, Burton A, Brady RL, Thomson AR, Woolfson DN J Am Chem Soc. 2019 May 8. doi: 10.1021/jacs.8b13354. PMID:31066556<ref>PMID:31066556</ref>

~~Description: Crystal structure~~ of ~~a CC~~-~~Hex mutant that forms an antiparallel four~~-~~helix coiled coil CC-Hex*-L24Dab~~

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

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

</div>

[[Category: Rhys, G.G]]

[[Category: Wood, C.W]]

== References ==

[[Category: ~~Brady~~, ~~R.L~~]]

[[Category: ~~Woolfson, D.N~~]]

__TOC__

[[Category: ~~Beesley, J.L~~]]

</StructureSection>

[[Category: Large Structures]]

[[Category: Beesley, J L]]

[[Category: Brady, R L]]

[[Category: Rhys, G G]]

[[Category: Wood, C W]]

[[Category: Woolfson, D N]]

[[Category: Antiparallel]]

[[Category: Cc-hex]]

[[Category: Coiled coil]]

[[Category: De novo protein]]

[[Category: Synthetic]]

[[Category: Tetramer]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6q5m is ON HOLD  until Paper Publication
+==Crystal structure of a CC-Hex mutant that forms an antiparallel four-helix coiled coil CC-Hex*-L24Dab==
+<StructureSection load='6q5m' size='340' side='right'caption='[[6q5m]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6q5m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q5M FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DAB:2,4-DIAMINOBUTYRIC+ACID'>DAB</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6q5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q5m OCA], [http://pdbe.org/6q5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q5m RCSB], [http://www.ebi.ac.uk/pdbsum/6q5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q5m ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The association of amphipathic alpha helices in water leads to alpha-helical-bundle protein structures. However, the driving force for this-the hydrophobic effect-is not specific and does not define the number or the orientation of helices in the associated state. Rather, this is achieved through deeper sequence-to-structure relationships, which are increas-ingly being discerned. For example, for one structurally extreme but nevertheless ubiquitous class of bundle-the alpha-helical coiled coils-relationships have been established that discriminate between all-parallel dimers, trimers and tetramers. Association states above this are known, as are antiparallel and mixed arrangements of the helices. However, these alternative states are less-well understood. Here, we describe a synthetic-peptide system that switches be-tween parallel hexamers and various up-down-up-down tetramers in response to single-amino-acid changes and solution conditions. The main accessible states of each peptide variant are characterized fully in solution and, in most cases, to high resolution with X-ray crystal structures. Analysis and inspection of these structures helps rationalize the different states formed. This navigation of the structural landscape of alpha-helical coiled coils above the dimers and tri-mers that dominate in nature has allowed us to design rationally a well-defined and hyperstable antiparallel coiled-coil tetramer (apCC-Tet). This robust de novo protein provides another scaffold for further structural and functional designs in protein engineering and synthetic biology.
-Authors: Wood, C.W., Beesley, J.L., Rhys, G.G., Brady, R.L., Woolfson, D.N.
+Navigating the structural landscape of de novo alpha-helical bundles.,Rhys GG, Wood CW, Beesley JL, Zaccai NR, Burton A, Brady RL, Thomson AR, Woolfson DN J Am Chem Soc. 2019 May 8. doi: 10.1021/jacs.8b13354. PMID:31066556<ref>PMID:31066556</ref>
-Description: Crystal structure of a CC-Hex mutant that forms an antiparallel four-helix coiled coil CC-Hex*-L24Dab
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Rhys, G.G]]
+<div class="pdbe-citations 6q5m" style="background-color:#fffaf0;"></div>
-[[Category: Wood, C.W]]
+== References ==
-[[Category: Brady, R.L]]
+<references/>
-[[Category: Woolfson, D.N]]
+__TOC__
-[[Category: Beesley, J.L]]
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Beesley, J L]]
+[[Category: Brady, R L]]
+[[Category: Rhys, G G]]
+[[Category: Wood, C W]]
+[[Category: Woolfson, D N]]
+[[Category: Antiparallel]]
+[[Category: Cc-hex]]
+[[Category: Coiled coil]]
+[[Category: De novo protein]]
+[[Category: Synthetic]]
+[[Category: Tetramer]]