This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4f3d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:19, 27 March 2019

Structure of RPE65: P65 crystal form grown in Fos-Choline-10

Structural highlights

4f3d is a 2 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, 4f30, 4f3a
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/4f3d"

@@ Line 1: / Line 1: @@
 ==Structure of RPE65: P65 crystal form grown in Fos-Choline-10==
-<StructureSection load='4f3d' size='340' side='right' caption='[[4f3d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='4f3d' size='340' side='right'caption='[[4f3d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4f3d]] is a 2 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=4F3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F3D FirstGlance]. <br>
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 4f3d" 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]]

4f3d

From Proteopedia

Revision as of 08:19, 27 March 2019

Structure of RPE65: P65 crystal form grown in Fos-Choline-10

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox