8drf: Difference between revisions
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==Zn(II)-bound B2 dimer (H60/H100/H104)== | |||
<StructureSection load='8drf' size='340' side='right'caption='[[8drf]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8drf]] is a 1 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=8DRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DRF FirstGlance]. <br> | |||
</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=8drf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8drf OCA], [https://pdbe.org/8drf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8drf RCSB], [https://www.ebi.ac.uk/pdbsum/8drf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8drf 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 == | |||
Selective metal binding is a key requirement not only for the functions of natural metalloproteins but also for the potential applications of artificial metalloproteins in heterogeneous environments such as cells and environmental samples. The selection of transition-metal ions through protein design can, in principle, be achieved through the appropriate choice and the precise positioning of amino acids that comprise the primary metal coordination sphere. However, this task is made difficult by the intrinsic flexibility of proteins and the fact that protein design approaches generally lack the sub-A precision required for the steric selection of metal ions. We recently introduced a flexible/probabilistic protein design strategy (MASCoT) that allows metal ions to search for optimal coordination geometry within a flexible, yet covalently constrained dimer interface. In an earlier proof-of-principle study, we used MASCoT to generate an artificial metalloprotein dimer, (AB)2, which selectively bound Co(II) and Ni(II) over Cu(II) (as well as other first-row transition-metal ions) through the imposition of a rigid octahedral coordination geometry, thus countering the Irving-Williams trend. In this study, we set out to redesign (AB)2 to examine the applicability of MASCoT to the selective binding of other metal ions. We report here the design and characterization of a new flexible protein dimer, B2, which displays Zn(II) selectivity over all other tested metal ions including Cu(II) both in vitro and in cellulo. Selective, anti-Irving-Williams Zn(II) binding by B2 is achieved through the formation of a unique trinuclear Zn coordination motif in which His and Glu residues are rigidly placed in a tetrahedral geometry. These results highlight the utility of protein flexibility in the design and discovery of selective binding motifs. | |||
Design of a Flexible, Zn-Selective Protein Scaffold that Displays Anti-Irving-Williams Behavior.,Choi TS, Tezcan FA J Am Chem Soc. 2022 Oct 5;144(39):18090-18100. doi: 10.1021/jacs.2c08050. Epub, 2022 Sep 26. PMID:36154053<ref>PMID:36154053</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8drf" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Choi TS]] | |||
[[Category: Tezcan FA]] |
Revision as of 22:36, 19 October 2022
Zn(II)-bound B2 dimer (H60/H100/H104)Zn(II)-bound B2 dimer (H60/H100/H104)
Structural highlights
FunctionC562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMedSelective metal binding is a key requirement not only for the functions of natural metalloproteins but also for the potential applications of artificial metalloproteins in heterogeneous environments such as cells and environmental samples. The selection of transition-metal ions through protein design can, in principle, be achieved through the appropriate choice and the precise positioning of amino acids that comprise the primary metal coordination sphere. However, this task is made difficult by the intrinsic flexibility of proteins and the fact that protein design approaches generally lack the sub-A precision required for the steric selection of metal ions. We recently introduced a flexible/probabilistic protein design strategy (MASCoT) that allows metal ions to search for optimal coordination geometry within a flexible, yet covalently constrained dimer interface. In an earlier proof-of-principle study, we used MASCoT to generate an artificial metalloprotein dimer, (AB)2, which selectively bound Co(II) and Ni(II) over Cu(II) (as well as other first-row transition-metal ions) through the imposition of a rigid octahedral coordination geometry, thus countering the Irving-Williams trend. In this study, we set out to redesign (AB)2 to examine the applicability of MASCoT to the selective binding of other metal ions. We report here the design and characterization of a new flexible protein dimer, B2, which displays Zn(II) selectivity over all other tested metal ions including Cu(II) both in vitro and in cellulo. Selective, anti-Irving-Williams Zn(II) binding by B2 is achieved through the formation of a unique trinuclear Zn coordination motif in which His and Glu residues are rigidly placed in a tetrahedral geometry. These results highlight the utility of protein flexibility in the design and discovery of selective binding motifs. Design of a Flexible, Zn-Selective Protein Scaffold that Displays Anti-Irving-Williams Behavior.,Choi TS, Tezcan FA J Am Chem Soc. 2022 Oct 5;144(39):18090-18100. doi: 10.1021/jacs.2c08050. Epub, 2022 Sep 26. PMID:36154053[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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