3qw0: Difference between revisions
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==Crystal structure of the Zn-RIDC1 complex stabilized by BMB crosslinks== | |||
<StructureSection load='3qw0' size='340' side='right'caption='[[3qw0]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qw0]] 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=3QW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QW0 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]] 1.84Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ME9:1,1-BUTANE-1,4-DIYLBIS(1H-PYRROLE-2,5-DIONE)'>ME9</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=3qw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw0 OCA], [https://pdbe.org/3qw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qw0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Here, we report that the approach of metal-templated ligand synthesis can be applied to construct a dimeric protein assembly ((BMOE)RIDC1(2)), which is stabilized by noncovalent interactions and flexible covalent cross-linkers around the Zn templates. Despite its flexibility, (BMOE)RIDC1(2) selectively binds Zn(II) over other divalent metals and undergoes dimerization upon metal binding. Such simultaneous fulfillment of plasticity and selectivity is a hallmark of cellular signaling events that involve ligand/metal-induced protein dimerization. | |||
Templated Construction of a Zn-Selective Protein Dimerization Motif.,Salgado EN, Brodin JD, To MM, Tezcan FA Inorg Chem. 2011 Jun 7. PMID:21648390<ref>PMID:21648390</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3qw0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Salgado EN]] | |||
[[Category: Tezcan FA]] | |||
Latest revision as of 09:42, 27 November 2024
Crystal structure of the Zn-RIDC1 complex stabilized by BMB crosslinksCrystal structure of the Zn-RIDC1 complex stabilized by BMB crosslinks
Structural highlights
Publication Abstract from PubMedHere, we report that the approach of metal-templated ligand synthesis can be applied to construct a dimeric protein assembly ((BMOE)RIDC1(2)), which is stabilized by noncovalent interactions and flexible covalent cross-linkers around the Zn templates. Despite its flexibility, (BMOE)RIDC1(2) selectively binds Zn(II) over other divalent metals and undergoes dimerization upon metal binding. Such simultaneous fulfillment of plasticity and selectivity is a hallmark of cellular signaling events that involve ligand/metal-induced protein dimerization. Templated Construction of a Zn-Selective Protein Dimerization Motif.,Salgado EN, Brodin JD, To MM, Tezcan FA Inorg Chem. 2011 Jun 7. PMID:21648390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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