2muz: Difference between revisions
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New page: '''Unreleased structure''' The entry 2muz is ON HOLD Authors: Wang, T., Joh, N., Wu, Y., DeGrado, W.F., Hong, M. Description: ssNMR structure of a designed rocker protein |
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The | ==ssNMR structure of a designed rocker protein== | ||
<StructureSection load='2muz' size='340' side='right'caption='[[2muz]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2muz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MUZ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PFF:4-FLUORO-L-PHENYLALANINE'>PFF</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=2muz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2muz OCA], [https://pdbe.org/2muz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2muz RCSB], [https://www.ebi.ac.uk/pdbsum/2muz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2muz ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The design of functional membrane proteins from first principles represents a grand challenge in chemistry and structural biology. Here, we report the design of a membrane-spanning, four-helical bundle that transports first-row transition metal ions Zn(2+) and Co(2+), but not Ca(2+), across membranes. The conduction path was designed to contain two di-metal binding sites that bind with negative cooperativity. X-ray crystallography and solid-state and solution nuclear magnetic resonance indicate that the overall helical bundle is formed from two tightly interacting pairs of helices, which form individual domains that interact weakly along a more dynamic interface. Vesicle flux experiments show that as Zn(2+) ions diffuse down their concentration gradients, protons are antiported. These experiments illustrate the feasibility of designing membrane proteins with predefined structural and dynamic properties. | |||
De novo design of a transmembrane Zn(2)(+)-transporting four-helix bundle.,Joh NH, Wang T, Bhate MP, Acharya R, Wu Y, Grabe M, Hong M, Grigoryan G, DeGrado WF Science. 2014 Dec 19;346(6216):1520-4. doi: 10.1126/science.1261172. PMID:25525248<ref>PMID:25525248</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2muz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: DeGrado WF]] | |||
[[Category: Hong M]] | |||
[[Category: Joh N]] | |||
[[Category: Wang T]] | |||
[[Category: Wu Y]] | |||
Latest revision as of 22:26, 26 March 2025
ssNMR structure of a designed rocker protein
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