6mqw: Difference between revisions
New page: '''Unreleased structure''' The entry 6mqw is ON HOLD Authors: Ghanbarpour, A., Geiger, J. Description: Crystal Structure of All-Trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L12... |
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The | ==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 (10 minutes) at 2.1 Angstrom Resolution== | ||
<StructureSection load='6mqw' size='340' side='right'caption='[[6mqw]], [[Resolution|resolution]] 2.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mqw]] 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=6MQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MQW 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]] 2.09Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6mqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mqw OCA], [https://pdbe.org/6mqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mqw RCSB], [https://www.ebi.ac.uk/pdbsum/6mqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mqw 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6mqw" style="background-color:#fffaf0;"></div> | ||
[[Category: Geiger | |||
==See Also== | |||
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Geiger J]] | |||
[[Category: Ghanbarpour A]] | |||
Latest revision as of 09:37, 11 October 2023
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 (10 minutes) at 2.1 Angstrom ResolutionCrystal 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 (10 minutes) at 2.1 Angstrom Resolution
Structural highlights
FunctionRABP2_HUMAN Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Publication Abstract from PubMedBacteriorhodopsin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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