5tgw
From Proteopedia
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==NMR structure of apo-PS1== | ==NMR structure of apo-PS1== | ||
| - | <StructureSection load='5tgw' size='340' side='right' caption='[[5tgw | + | <StructureSection load='5tgw' size='340' side='right'caption='[[5tgw]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5tgw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGW OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5tgw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TGW FirstGlance]. <br> |
| - | </td></tr> | + | </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=5tgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tgw OCA], [https://pdbe.org/5tgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tgw RCSB], [https://www.ebi.ac.uk/pdbsum/5tgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tgw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein catalysis requires the atomic-level orchestration of side chains, substrates and cofactors, and yet the ability to design a small-molecule-binding protein entirely from first principles with a precisely predetermined structure has not been demonstrated. Here we report the design of a novel protein, PS1, that binds a highly electron-deficient non-natural porphyrin at temperatures up to 100 degrees C. The high-resolution structure of holo-PS1 is in sub-A agreement with the design. The structure of apo-PS1 retains the remote core packing of the holoprotein, with a flexible binding region that is predisposed to ligand binding with the desired geometry. Our results illustrate the unification of core packing and binding-site definition as a central principle of ligand-binding protein design. | ||
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| + | De novo design of a hyperstable non-natural protein-ligand complex with sub-A accuracy.,Polizzi NF, Wu Y, Lemmin T, Maxwell AM, Zhang SQ, Rawson J, Beratan DN, Therien MJ, DeGrado WF Nat Chem. 2017 Dec;9(12):1157-1164. doi: 10.1038/nchem.2846. Epub 2017 Aug 21. PMID:29168496<ref>PMID:29168496</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5tgw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Polizzi NF]] |
| - | [[Category: | + | [[Category: Wu Y]] |
| - | + | ||
Current revision
NMR structure of apo-PS1
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