4YD8
Bardet-Biedl Syndrome 9 Protein (aa1-407), Homo sapiens
Summary for 4YD8
| Entry DOI | 10.2210/pdb4yd8/pdb |
| Descriptor | Protein PTHB1 (2 entities in total) |
| Functional Keywords | beta propeller, structural protein, bbsome, coat complex, protein transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 93035.67 |
| Authors | Knockenhauer, K.E.,Schwartz, T.U. (deposition date: 2015-02-21, release date: 2015-06-24, Last modification date: 2024-11-06) |
| Primary citation | Knockenhauer, K.E.,Schwartz, T.U. Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9). J.Biol.Chem., 290:19569-19583, 2015 Cited by PubMed Abstract: The Bardet-Biedl syndrome protein complex (BBSome) is an octameric complex that transports membrane proteins into the primary cilium signaling organelle in eukaryotes and is implicated in human disease. Here we have analyzed the 99-kDa human BBS9 protein, one of the eight BBSome components. The protein is composed of four structured domains, including a β-stranded N-terminal domain. The 1.8 Å crystal structure of the 46-kDa N-terminal domain reveals a seven-bladed β-propeller. A structure-based homology search suggests that it functions in protein-protein interactions. We show that the Bardet-Biedl syndrome-causing G141R mutation in BBS9 likely results in misfolding of the β-propeller. Although the C-terminal half of BBS9 dimerizes in solution, the N-terminal domain only does so in the crystal lattice. This C-terminal dimerization interface might be important for the assembly of the BBSome. PubMed: 26085087DOI: 10.1074/jbc.M115.649202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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