1uw1
From Proteopedia
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| - | [[Image:1uw1.jpg|left|200px]] | ||
| - | + | ==A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution== | |
| - | + | <StructureSection load='1uw1' size='340' side='right'caption='[[1uw1]], [[Resolution|resolution]] 1.94Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1uw1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UW1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1uw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uw1 OCA], [https://pdbe.org/1uw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uw1 RCSB], [https://www.ebi.ac.uk/pdbsum/1uw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uw1 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion. | A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion. | ||
| - | + | A novel ADP- and zinc-binding fold from function-directed in vitro evolution.,Lo Surdo P, Walsh MA, Sollazzo M Nat Struct Mol Biol. 2004 Apr;11(4):382-3. Epub 2004 Mar 14. PMID:15024384<ref>PMID:15024384</ref> | |
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| - | A novel ADP- and zinc-binding fold from function-directed in vitro evolution., Lo Surdo P, Walsh MA, Sollazzo M | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1uw1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Lo Surdo P]] | ||
| + | [[Category: Sollazzo M]] | ||
| + | [[Category: Walsh MA]] | ||
Current revision
A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution
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