4f3a

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==Structure of RPE65: P6522 crystal form, iridium derivative==
==Structure of RPE65: P6522 crystal form, iridium derivative==
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<StructureSection load='4f3a' size='340' side='right' caption='[[4f3a]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='4f3a' size='340' side='right'caption='[[4f3a]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f3a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F3A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F3A FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fsn|3fsn]], [[4f2z|4f2z]], [[4f30|4f30]], [[4f3d|4f3d]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Retinoid_isomerohydrolase Retinoid isomerohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.64 3.1.1.64] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3a OCA], [https://pdbe.org/4f3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f3a RCSB], [https://www.ebi.ac.uk/pdbsum/4f3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f3a ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f3a RCSB], [http://www.ebi.ac.uk/pdbsum/4f3a PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/RPE65_BOVIN RPE65_BOVIN] Plays important roles in the production of 11-cis retinal and in visual pigment regeneration. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT. The enzymatic activity is linearly dependent of the expression levels and membrane association.<ref>PMID:16096063</ref> <ref>PMID:19805034</ref> <ref>PMID:20100834</ref>
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== Publication Abstract from PubMed ==
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RPE65 is a key metalloenzyme responsible for maintaining visual function in vertebrates. Despite extensive research on this membrane-bound retinoid isomerase, fundamental questions regarding its enzymology remain unanswered. Here, we report the crystal structure of RPE65 in a membrane-like environment. These crystals, obtained from enzymatically active, nondelipidated protein, displayed an unusual packing arrangement wherein RPE65 is embedded in a lipid-detergent sheet. Structural differences between delipidated and nondelipidated RPE65 uncovered key residues involved in substrate uptake and processing. Complementary iron K-edge X-ray absorption spectroscopy data established that RPE65 as isolated contained a divalent iron center and demonstrated the presence of a tightly bound ligand consistent with a coordinated carboxylate group. These results support the hypothesis that the Lewis acidity of iron could be used to promote ester dissociation and generation of a carbocation intermediate required for retinoid isomerization.
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Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis.,Kiser PD, Farquhar ER, Shi W, Sui X, Chance MR, Palczewski K Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):E2747-56. doi:, 10.1073/pnas.1212025109. Epub 2012 Sep 24. PMID:23012475<ref>PMID:23012475</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Retinoid isomerohydrolase|Retinoid isomerohydrolase]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Retinoid isomerohydrolase]]
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[[Category: Large Structures]]
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[[Category: Kiser, P D.]]
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[[Category: Kiser PD]]
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[[Category: Palczewski, K.]]
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[[Category: Palczewski K]]
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[[Category: Beta-propeller]]
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[[Category: Hydrolase]]
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[[Category: Isomerase]]
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[[Category: Metalloprotein]]
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[[Category: Monotopic membrane protein]]
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[[Category: Non-heme iron protein]]
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[[Category: Smooth er membrane]]
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Current revision

Structure of RPE65: P6522 crystal form, iridium derivative

PDB ID 4f3a

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