1wr0: Difference between revisions

Revision as of 16:47, 21 February 2008

Structural characterization of the MIT domain from human Vps4b

OverviewOverview

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.

About this StructureAbout this Structure

1WR0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural characterization of the MIT domain from human Vps4b., Takasu H, Jee JG, Ohno A, Goda N, Fujiwara K, Tochio H, Shirakawa M, Hiroaki H, Biochem Biophys Res Commun. 2005 Aug 26;334(2):460-5. PMID:16018968

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 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 16: / Line 16: @@
 [[Category: Goda, N.]]
 [[Category: Hiroaki, H.]]
-[[Category: Jee, J.G.]]
+[[Category: Jee, J G.]]
 [[Category: Ohno, A.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Shirakawa, M.]]
 [[Category: Takasu, H.]]
@@ Line 35: / Line 35: @@
 [[Category: vps4b]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:55:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:17 2008''