5ubs: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ubs is ON HOLD  until Paper Publication
+==Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43==
+<StructureSection load='5ubs' size='340' side='right'caption='[[5ubs]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ubs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._GX7805 Streptococcus sp. GX7805]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UBS 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=5ubs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ubs OCA], [https://pdbe.org/5ubs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ubs RCSB], [https://www.ebi.ac.uk/pdbsum/5ubs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ubs ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Proteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain beta1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states.
-Authors:
+Rational design of proteins that exchange on functional timescales.,Davey JA, Damry AM, Goto NK, Chica RA Nat Chem Biol. 2017 Oct 23. doi: 10.1038/nchembio.2503. PMID:29058725<ref>PMID:29058725</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 5ubs" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Protein G|Protein G]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptococcus sp. GX7805]]
+[[Category: Chica RA]]
+[[Category: Damry AM]]
+[[Category: Davey JA]]
+[[Category: Goto NK]]