Summary for 6CMY
| Entry DOI | 10.2210/pdb6cmy/pdb |
| NMR Information | BMRB: 30101 |
| Descriptor | Melanoregulin (1 entity in total) |
| Functional Keywords | alpha helical, crac motif, melanosome transport, cellular pigementation, dilute suppressor locus, lipid binding protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 21364.21 |
| Authors | Rout, A.K.,Wu, X.,Strub, M.P.,Starich, M.R.,Hammer III, J.A.,Tjandra, N. (deposition date: 2018-03-06, release date: 2018-09-19, Last modification date: 2024-05-15) |
| Primary citation | Rout, A.K.,Wu, X.,Starich, M.R.,Strub, M.P.,Hammer, J.A.,Tjandra, N. The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function. Structure, 26:1373-, 2018 Cited by PubMed Abstract: 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 α 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. PubMed: 30174147DOI: 10.1016/j.str.2018.07.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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