6cmy

Solution NMR Structure Determination of Mouse MelanoregulinSolution NMR Structure Determination of Mouse Melanoregulin

Structural highlights

6cmy is a 1 chain structure with sequence from Mus musculus. This structure supersedes the now removed PDB entry 5kbo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MREG_MOUSE Plays a role in the incorporation of pigments into hair. May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells.^[1] ^[2]

Publication Abstract from PubMed

Melanoregulin (Mreg) is a small, highly charged, multiply palmitoylated protein present on the membrane of melanosomes. Mreg is implicated in the transfer of melanosomes from melanocytes to keratinocytes, and in promoting the microtubule minus end-directed transport of these organelles. The possible molecular function of Mreg was identified by solving its structure using nuclear magnetic resonance (NMR) spectroscopy. Mreg contains six alpha helices forming a fishhook-like fold in which positive and negative charges occupy opposite sides of the protein's surface and sandwich a putative, cholesterol recognition sequence (CRAC motif). Mreg containing a point mutation within its CRAC motif still targets to late endosomes/lysosomes, but no longer promotes their microtubule minus end-directed transport. Moreover, wild-type Mreg does not promote the microtubule minus end-directed transport of late endosomes/lysosomes in cells transiently depleted of cholesterol. Finally, reversing the charge of three clustered acidic residues partially inhibits Mreg's ability to drive these organelles to microtubule minus ends.

The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function.,Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ O'Sullivan TN, Wu XS, Rachel RA, Huang JD, Swing DA, Matesic LE, Hammer JA 3rd, Copeland NG, Jenkins NA. dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice. Proc Natl Acad Sci U S A. 2004 Nov 30;101(48):16831-6. Epub 2004 Nov 18. PMID:15550542 doi:http://dx.doi.org/10.1073/pnas.0407339101
↑ Boesze-Battaglia K, Song H, Sokolov M, Lillo C, Pankoski-Walker L, Gretzula C, Gallagher B, Rachel RA, Jenkins NA, Copeland NG, Morris F, Jacob J, Yeagle P, Williams DS, Damek-Poprawa M. The tetraspanin protein peripherin-2 forms a complex with melanoregulin, a putative membrane fusion regulator. Biochemistry. 2007 Feb 6;46(5):1256-72. PMID:17260955 doi:http://dx.doi.org/10.1021/bi061466i
↑ Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N. The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function. Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147 doi:http://dx.doi.org/10.1016/j.str.2018.07.009

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OCA

[1] O'Sullivan TN, Wu XS, Rachel RA, Huang JD, Swing DA, Matesic LE, Hammer JA 3rd, Copeland NG, Jenkins NA. dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice. Proc Natl Acad Sci U S A. 2004 Nov 30;101(48):16831-6. Epub 2004 Nov 18. PMID:15550542 doi:http://dx.doi.org/10.1073/pnas.0407339101

[2] Boesze-Battaglia K, Song H, Sokolov M, Lillo C, Pankoski-Walker L, Gretzula C, Gallagher B, Rachel RA, Jenkins NA, Copeland NG, Morris F, Jacob J, Yeagle P, Williams DS, Damek-Poprawa M. The tetraspanin protein peripherin-2 forms a complex with melanoregulin, a putative membrane fusion regulator. Biochemistry. 2007 Feb 6;46(5):1256-72. PMID:17260955 doi:http://dx.doi.org/10.1021/bi061466i

[3] Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N. The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function. Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147 doi:http://dx.doi.org/10.1016/j.str.2018.07.009

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