4u9d: Difference between revisions
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==Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3== | ==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=''> | <StructureSection load='4u9d' size='340' side='right'caption='[[4u9d]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == 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 [ | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4u9d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Song WJ]] | ||
[[Category: | [[Category: Tezcan FA]] | ||
Latest revision as of 03:50, 28 December 2023
Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3Crystal Structure of the Zn-directed tetramer of the engineered cyt cb562 variant, AB3
Structural highlights
FunctionC562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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