5e6g: Difference between revisions

Line 1:

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

~~The entry~~ 5e6g is ~~ON HOLD until Paper~~ Publication

==Crystal Structure of De Novo Designed Protein CA01==

== Structural highlights ==

<table><tr><td colspan='2'>[[5e6g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6G FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6g OCA], [http://pdbe.org/5e6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6g RCSB], [http://www.ebi.ac.uk/pdbsum/5e6g PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100 degrees C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds.

~~Authors:~~ Jacobs, T~~.M.~~, ~~Williams~~, T., Kuhlman, B.

Design of structurally distinct proteins using strategies inspired by evolution.,Jacobs TM, Williams B, Williams T, Xu X, Eletsky A, Federizon JF, Szyperski T, Kuhlman B Science. 2016 May 6;352(6286):687-90. doi: 10.1126/science.aad8036. PMID:27151863<ref>PMID:27151863</ref>

~~Description: Crystal Structure~~ of ~~De Novo Designed Protein CA01~~

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

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

</div>

[[Category: Jacobs, T.M]]

== References ==

__TOC__

</StructureSection>

[[Category: Jacobs, T M]]

[[Category: Kuhlman, B]]

[[Category: Williams, T]]

[[Category: Computational design]]

[[Category: De novo protein]]

[[Category: Protein engineering]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5e6g is ON HOLD  until Paper Publication
+==Crystal Structure of De Novo Designed Protein CA01==
+<StructureSection load='5e6g' size='340' side='right' caption='[[5e6g]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5e6g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6G FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5e6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6g OCA], [http://pdbe.org/5e6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6g RCSB], [http://www.ebi.ac.uk/pdbsum/5e6g PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100 degrees C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds.
-Authors: Jacobs, T.M., Williams, T., Kuhlman, B.
+Design of structurally distinct proteins using strategies inspired by evolution.,Jacobs TM, Williams B, Williams T, Xu X, Eletsky A, Federizon JF, Szyperski T, Kuhlman B Science. 2016 May 6;352(6286):687-90. doi: 10.1126/science.aad8036. PMID:27151863<ref>PMID:27151863</ref>
-Description: Crystal Structure of De Novo Designed Protein CA01
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Jacobs, T.M]]
+<div class="pdbe-citations 5e6g" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Jacobs, T M]]
 [[Category: Kuhlman, B]]
 [[Category: Williams, T]]
+[[Category: Computational design]]
+[[Category: De novo protein]]
+[[Category: Protein engineering]]