View source for 6mqx


==Crystal Structure of All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Human Cellular Retinoic Acid Binding Protein II Irradiated with 400 nm Laser (30 seconds) and Subsequently Dark Adapted (25 minutes) at 2.0 Angstrom Resolution==
<StructureSection load='6mqx' size='340' side='right'caption='[[6mqx]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MQX 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]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=6mqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mqx OCA], [https://pdbe.org/6mqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mqx RCSB], [https://www.ebi.ac.uk/pdbsum/6mqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mqx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RABP2_HUMAN RABP2_HUMAN] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmem-brane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodop-sin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. Described is a microbial rhodopsin mimic, created using a small soluble protein as template, that specifically photo-isomerizes all-trans to 13-cis retinal followed by thermal relaxation to the all-trans isomer, mimicking the bacteriorhodopsin photocycle, in a single crystal. The key element for selective isomerization is a tuned steric interaction between chromophore and protein, similar to that seen in the microbial rhodopsins. It is further demonstrated that a single mutation converts the system into a protein photo-switch without chromophore photoisomerization or conformational change.

Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.,Ghanbarpour A, Nairat M, Nosrati M, Santos EM, Vasileiou C, Dantus M, Borhan B, Geiger JH J Am Chem Soc. 2018 Dec 22. doi: 10.1021/jacs.8b12493. PMID:30580520<ref>PMID:30580520</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mqx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Geiger J]]
[[Category: Ghanbarpour A]]