4p6j

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'''Unreleased structure'''
 
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The entry 4p6j is ON HOLD until Paper Publication
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==Crystal Structure of the Computationally Designed Transmembrane Metallotransporter with 4-bromophenylalanine in Octyl Glucoside==
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<StructureSection load='4p6j' size='340' side='right'caption='[[4p6j]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4p6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P6J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4BF:4-BROMO-L-PHENYLALANINE'>4BF</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6j OCA], [https://pdbe.org/4p6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p6j RCSB], [https://www.ebi.ac.uk/pdbsum/4p6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6j ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Joh, N.H., Acharya, R., DeGrado, W.F.
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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>
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Description: Crystal Structure of the Computationally Designed Transmembrane Metallotransporter with 4-bromophenylalanine in Octyl Glucoside
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4p6j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Acharya R]]
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[[Category: DeGrado WF]]
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[[Category: Joh NH]]

Current revision

Crystal Structure of the Computationally Designed Transmembrane Metallotransporter with 4-bromophenylalanine in Octyl Glucoside

PDB ID 4p6j

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