4f30: Difference between revisions
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==Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution== | ==Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution== | ||
<StructureSection load='4f30' size='340' side='right' caption='[[4f30]], [[Resolution|resolution]] 3.15Å' scene=''> | <StructureSection load='4f30' size='340' side='right'caption='[[4f30]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f30]] 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=4F30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F30 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4f30]] 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=4F30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F30 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4f30" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4f30" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Retinoid isomerohydrolase|Retinoid isomerohydrolase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Retinoid isomerohydrolase]] | [[Category: Retinoid isomerohydrolase]] | ||
[[Category: Kiser, P D]] | [[Category: Kiser, P D]] | ||
Revision as of 10:36, 27 March 2019
Structure of RPE65: P6522 crystal form grown in ammonium phosphate solutionStructure of RPE65: P6522 crystal form grown in ammonium phosphate solution
Structural highlights
Function[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.[1] [2] [3] Publication Abstract from PubMedRPE65 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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