4zgu

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<table><tr><td colspan='2'>[[4zgu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZGU FirstGlance]. <br>
<table><tr><td colspan='2'>[[4zgu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZGU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<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=4zgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgu OCA], [http://pdbe.org/4zgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zgu RCSB], [http://www.ebi.ac.uk/pdbsum/4zgu PDBsum]</span></td></tr>
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<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=4zgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgu OCA], [http://pdbe.org/4zgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zgu RCSB], [http://www.ebi.ac.uk/pdbsum/4zgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Protein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. This system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. With only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum.
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Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Herein we report that hCRBPII forms an extensive domain-swapped dimer during bacterial expression. The domain-swapped region encompasses almost half of the protein. The dimer represents a novel structural architecture with the mouths of the two binding cavities facing each other, producing a new binding cavity that spans the length of the protein complex. Although wild-type hCRBPII forms the dimer, the propensity for dimerization can be substantially increased via mutation at Tyr60. The monomeric form of the wild-type protein represents the thermodynamically more stable species, making the domain-swapped dimer a kinetically trapped entity. Hypothetically, the wild-type protein has evolved to minimize dimerization of the folding intermediate through a critical hydrogen bond (Tyr60-Glu72) that disfavors the dimeric form.
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Tuning the electronic absorption of protein-embedded all-trans-retinal.,Wang W, Nossoni Z, Berbasova T, Watson CT, Yapici I, Lee KS, Vasileiou C, Geiger JH, Borhan B Science. 2012 Dec 7;338(6112):1340-3. doi: 10.1126/science.1226135. PMID:23224553<ref>PMID:23224553</ref>
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Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.,Assar Z, Nossoni Z, Wang W, Santos EM, Kramer K, McCornack C, Vasileiou C, Borhan B, Geiger JH Structure. 2016 Sep 6;24(9):1590-8. doi: 10.1016/j.str.2016.05.022. Epub 2016 Aug, 11. PMID:27524203<ref>PMID:27524203</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4zgu" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4zgu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Retinol-binding protein|Retinol-binding protein]]
== References ==
== References ==
<references/>
<references/>

Revision as of 03:54, 6 September 2017

Crystal structure of monomer Y60W hCRBPII

4zgu, resolution 1.49Å

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