View source for 6mop


==Crystal Structure of the All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Mutant of Human Cellular Retinoic Acid Binding Protein II in the Dark at 1.9 Angstrom Resolution==
<StructureSection load='6mop' size='340' side='right' caption='[[6mop]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mop]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MOP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mop OCA], [http://pdbe.org/6mop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mop RCSB], [http://www.ebi.ac.uk/pdbsum/6mop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mop 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 6mop" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geiger, J]]
[[Category: Ghanbarpour, A]]
[[Category: Ilbp]]
[[Category: Lipid binding protein]]
[[Category: Rhodopsin mimic]]