1WR0
Structural characterization of the MIT domain from human Vps4b
Summary for 1WR0
| Entry DOI | 10.2210/pdb1wr0/pdb |
| Descriptor | SKD1 protein (1 entity in total) |
| Functional Keywords | vps4b, skd1, mit domain, escort, mvb, snps, protein transport, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi |
| Biological source | Homo sapiens (human) |
| Cellular location | Prevacuolar compartment membrane; Peripheral membrane protein: O75351 |
| Total number of polymer chains | 1 |
| Total formula weight | 9207.31 |
| Authors | Takasu, H.,Jee, J.G.,Ohno, A.,Goda, N.,Fujiwara, K.,Tochio, H.,Shirakawa, M.,Hiroaki, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-10-07, release date: 2005-08-02, Last modification date: 2024-05-29) |
| Primary citation | Takasu, H.,Jee, J.G.,Ohno, A.,Goda, N.,Fujiwara, K.,Tochio, H.,Shirakawa, M.,Hiroaki, H. Structural characterization of the MIT domain from human Vps4b Biochem.Biophys.Res.Commun., 334:460-465, 2005 Cited by PubMed Abstract: The microtubule interacting and trafficking (MIT) domain is a small protein module of unknown function that is conserved in proteins of diverse function, such as Vps4, sorting nexin 15 (SNX15), and spastin. One non-synonymous single nucleotide polymorphism was reported, which results in a Ile58-to-Met (I58M) substitution in hVps4b. Here, we have determined the solution structure of the MIT domain isolated from the NH(2)-terminus of human Vps4b, an AAA-ATPase involved in multivesicular body formation. The MIT domain adopts an 'up-and-down' three-helix bundle. Comparison with the sequences of other MIT domains clearly shows that the residues involved in inter-helical contacts are well conserved. The Ile58-to-Met substitution resulted a substantial thermal instability. In addition, we found a shallow crevice between helices A and C that may serve as a protein-binding site. We propose that the MIT domain serves as a putative adaptor domain for the ESCRT-III complex involved in endosomal trafficking. PubMed: 16018968DOI: 10.1016/j.bbrc.2005.06.110 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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