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4f30

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Revision as of 07:36, 27 March 2019

Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution

Structural highlights

4f30 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3fsn, 4f2z, 4f3a, 4f3d
Activity:	Retinoid isomerohydrolase, with EC number 3.1.1.64
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

References

↑ Jin M, Li S, Moghrabi WN, Sun H, Travis GH. Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium. Cell. 2005 Aug 12;122(3):449-59. PMID:16096063 doi:10.1016/j.cell.2005.06.042
↑ Kiser PD, Golczak M, Lodowski DT, Chance MR, Palczewski K. Crystal structure of native RPE65, the retinoid isomerase of the visual cycle. Proc Natl Acad Sci U S A. 2009 Oct 13;106(41):17325-30. Epub 2009 Oct 5. PMID:19805034
↑ Golczak M, Kiser PD, Lodowski DT, Maeda A, Palczewski K. Importance of membrane structural integrity for RPE65 retinoid isomerization activity. J Biol Chem. 2010 Mar 26;285(13):9667-82. Epub 2010 Jan 25. PMID:20100834 doi:10.1074/jbc.M109.063941
↑ Kiser PD, Farquhar ER, Shi W, Sui X, Chance MR, Palczewski K. Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. 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 doi:http://dx.doi.org/10.1073/pnas.1212025109

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4f30"

@@ Line 1: / Line 1: @@
 ==Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution==
-<StructureSection load='4f30' size='340' side='right' caption='[[4f30]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
+<StructureSection load='4f30' size='340' side='right'caption='[[4f30]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
 == 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>
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 4f30" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Retinoid isomerohydrolase|Retinoid isomerohydrolase]]
 == References ==
 <references/>
@@ Line 25: / Line 28: @@
 </StructureSection>
 [[Category: Bos taurus]]
+[[Category: Large Structures]]
 [[Category: Retinoid isomerohydrolase]]
 [[Category: Kiser, P D]]

4f30

From Proteopedia

Revision as of 07:36, 27 March 2019

Structure of RPE65: P6522 crystal form grown in ammonium phosphate solution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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