View source for 6mqy


==Crystal Structure of the 13-cis Product of All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Mutant of Human Cellular Retinoic Acid Binding Protein II Irradiated with 400 nm Laser (30 seconds) at 1.9 Angstrom==
<StructureSection load='6mqy' size='340' side='right'caption='[[6mqy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mqy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MQY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRABP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6mqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mqy OCA], [http://pdbe.org/6mqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mqy RCSB], [http://www.ebi.ac.uk/pdbsum/6mqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mqy ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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 6mqy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Geiger, J]]
[[Category: Ghanbarpour, A]]
[[Category: Ilbp]]
[[Category: Lipid binding protein]]
[[Category: Rhodopsin mimic]]