6vg7: Difference between revisions

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

~~The entry~~ 6vg7 is ~~ON HOLD until Paper~~ Publication

==De novo designed Rossmann fold protein ROS2_49223==

== Structural highlights ==

<table><tr><td colspan='2'>[[6vg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VG7 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vg7 OCA], [https://pdbe.org/6vg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vg7 RCSB], [https://www.ebi.ac.uk/pdbsum/6vg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vg7 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Naturally occurring proteins vary the precise geometries of structural elements to create distinct shapes optimal for function. We present a computational design method, loop-helix-loop unit combinatorial sampling (LUCS), that mimics nature's ability to create families of proteins with the same overall fold but precisely tunable geometries. Through near-exhaustive sampling of loop-helix-loop elements, LUCS generates highly diverse geometries encompassing those found in nature but also surpassing known structure space. Biophysical characterization showed that 17 (38%) of 45 tested LUCS designs encompassing two different structural topologies were well folded, including 16 with designed non-native geometries. Four experimentally solved structures closely matched the designs. LUCS greatly expands the designable structure space and offers a new paradigm for designing proteins with tunable geometries that may be customizable for novel functions.

~~Authors~~:

Expanding the space of protein geometries by computational design of de novo fold families.,Pan X, Thompson MC, Zhang Y, Liu L, Fraser JS, Kelly MJS, Kortemme T Science. 2020 Aug 28;369(6507):1132-1136. doi: 10.1126/science.abc0881. PMID:32855341<ref>PMID:32855341</ref>

~~Description~~:

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

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

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Kelly M]]

[[Category: Kortemme T]]

[[Category: Pan X]]

[[Category: Zhang Y]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6vg7 is ON HOLD  until Paper Publication
+==De novo designed Rossmann fold protein ROS2_49223==
+<StructureSection load='6vg7' size='340' side='right'caption='[[6vg7]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6vg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VG7 FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vg7 OCA], [https://pdbe.org/6vg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vg7 RCSB], [https://www.ebi.ac.uk/pdbsum/6vg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vg7 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Naturally occurring proteins vary the precise geometries of structural elements to create distinct shapes optimal for function. We present a computational design method, loop-helix-loop unit combinatorial sampling (LUCS), that mimics nature's ability to create families of proteins with the same overall fold but precisely tunable geometries. Through near-exhaustive sampling of loop-helix-loop elements, LUCS generates highly diverse geometries encompassing those found in nature but also surpassing known structure space. Biophysical characterization showed that 17 (38%) of 45 tested LUCS designs encompassing two different structural topologies were well folded, including 16 with designed non-native geometries. Four experimentally solved structures closely matched the designs. LUCS greatly expands the designable structure space and offers a new paradigm for designing proteins with tunable geometries that may be customizable for novel functions.
-Authors:
+Expanding the space of protein geometries by computational design of de novo fold families.,Pan X, Thompson MC, Zhang Y, Liu L, Fraser JS, Kelly MJS, Kortemme T Science. 2020 Aug 28;369(6507):1132-1136. doi: 10.1126/science.abc0881. PMID:32855341<ref>PMID:32855341</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 6vg7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Kelly M]]
+[[Category: Kortemme T]]
+[[Category: Pan X]]
+[[Category: Zhang Y]]