4p6k

<StructureSection load='4p6k' size='340' side='right' caption='[[4p6k]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[4p6k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6K FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4BF:4-BROMO-L-PHENYLALANINE'>4BF</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p6j|4p6j]], [[4p6l|4p6l]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6k OCA], [http://pdbe.org/4p6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p6k RCSB], [http://www.ebi.ac.uk/pdbsum/4p6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6k ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4p6k" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Acharya, R]]

[[Category: DeGrado, W F]]

[[Category: Joh, N H]]

[[Category: De novo protein]]

[[Category: De-novo designed]]

[[Category: Transporter]]