4u9d: Difference between revisions

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New page: '''Unreleased structure''' The entry 4u9d is ON HOLD Authors: Tezcan, F. A., Song, W. J. Description:
 
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'''Unreleased structure'''


The entry 4u9d is ON HOLD
==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]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4u9d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4U9D 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=4u9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9d OCA], [https://pdbe.org/4u9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u9d RCSB], [https://www.ebi.ac.uk/pdbsum/4u9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u9d ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.


Authors: Tezcan, F. A., Song, W. J.
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>


Description:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4u9d" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Song WJ]]
[[Category: Tezcan FA]]
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