3fsn | pdb_00003fsn

Crystal structure of RPE65 at 2.14 angstrom resolution

spinqualitylabelsall models 3fsn, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fsn is a 2 chain structure with sequence from Bos taurus. The March 2012 RCSB PDB Molecule of the Month feature on Rhodopsin by David Goodsell is 10.2210/rcsb_pdb/mom_2012_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE2, PG4 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Vertebrate vision is maintained by the retinoid (visual) cycle, a complex enzymatic pathway that operates in the retina to regenerate the visual chromophore, 11-cis-retinal. A key enzyme in this pathway is the microsomal membrane protein RPE65. This enzyme catalyzes the conversion of all-trans-retinyl esters to 11-cis-retinol in the retinal pigment epithelium (RPE). Mutations in RPE65 are known to be responsible for a subset of cases of the most common form of childhood blindness, Leber congenital amaurosis (LCA). Although retinoid isomerase activity has been attributed to RPE65, its catalytic mechanism remains a matter of debate. Also, the manner in which RPE65 binds to membranes and extracts retinoid substrates is unclear. To gain insight into these questions, we determined the crystal structure of native bovine RPE65 at 2.14-A resolution. The structural, biophysical, and biochemical data presented here provide the framework needed for an in-depth understanding of the mechanism of catalytic isomerization and membrane association, in addition to the role mutations that cause LCA have in disrupting protein function. Crystal structure of native RPE65, the retinoid isomerase of the visual cycle.,Kiser PD, Golczak M, Lodowski DT, Chance MR, Palczewski K Proc Natl Acad Sci U S A. 2009 Oct 13;106(41):17325-30. Epub 2009 Oct 5. PMID:19805034 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinoid isomerohydrolase

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