4u9d
From Proteopedia
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| - | ''' | + | ==Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3== |
| + | <StructureSection load='4u9d' size='340' side='right' caption='[[4u9d]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4u9d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U9D FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u9d RCSB], [http://www.ebi.ac.uk/pdbsum/4u9d PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-beta-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-beta-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 x 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural beta-lactamases to enable substrate interactions. | ||
| - | + | A designed supramolecular protein assembly with in vivo enzymatic activity.,Song WJ, Tezcan FA Science. 2014 Dec 19;346(6216):1525-8. doi: 10.1126/science.1259680. PMID:25525249<ref>PMID:25525249</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Tezcan, F | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Song, W J]] | ||
| + | [[Category: Tezcan, F A]] | ||
| + | [[Category: Designed enzyme]] | ||
| + | [[Category: Tetramer assembly]] | ||
| + | [[Category: Zn-coordinating protein]] | ||
Revision as of 13:36, 14 January 2015
Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3
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