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-Structure paper
Title | Structure of the human Meckel-Gruber protein Meckelin. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 45, Page eabj9748, Year 2021 |
Publish date | Nov 5, 2021 |
Authors | Dongliang Liu / Dandan Qian / Huaizong Shen / Deshun Gong / |
PubMed Abstract | Mutations in the gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate. Here, we report a 3.3-Å cryo–electron microscopy structure of ...Mutations in the gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate. Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3). The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain. Meckelin forms a stable homodimer with an extensive dimer interface. Our structure establishes a framework for dissecting the function and disease mechanisms of Meckelin. |
External links | Sci Adv / PubMed:34731008 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.34 Å |
Structure data | EMDB-31584, PDB-7fh1: |
Source |
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Keywords | MEMBRANE PROTEIN / Cryo-EM |