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- 저자 : Tsukihara, Tomitake (검색결과 3 건)
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Nishio, Kazuya,Ogasahara, Kyoko,Morimoto, Yukio,Tsukihara, Tomitake,Lee, Soo Jae,Yutani, Katsuhide Blackwell Publishing Ltd 2010 FEBS JOURNAL Vol.277 No.9
<P>To understand the basis for the lower activity of the tryptophan synthase β<SUB>2</SUB> subunit in comparison to the α<SUB>2</SUB>β<SUB>2</SUB> complex, we determined the crystal structures of apo‐β<SUB>2</SUB> and holo‐β<SUB>2</SUB> from <I>Escherichia coli</I> at 3.0 and 2.9 Å resolutions, respectively. To our knowledge, this is the first report of both β<SUB>2</SUB> subunit structures with and without pyridoxal‐5′‐phosphate. The apo‐type molecule retained a dimeric form in solution, as in the case of the holo‐β<SUB>2</SUB> subunit. The subunit structures of both the apo‐β<SUB>2</SUB> and the holo‐β<SUB>2</SUB> forms consisted of two domains, namely the N domain and the C domain. Although there were significant structural differences between the apo‐ and holo‐structures, they could be easily superimposed with a 22° rigid body rotation of the C domain. The pyridoxal‐5′‐phosphate‐bound holo‐form had multiple interactions between the two domains and a long loop (residues 260–310), which were missing in the apo‐form. Comparison of the structures of holo‐<I>Ec</I>β<SUB>2</SUB> and <I>St</I>β<SUB>2</SUB> in the α<SUB>2</SUB>β<SUB>2</SUB> complex from <I>Salmonella typhimurium</I> (<I>St</I>α<SUB>2</SUB>β<SUB>2</SUB>) identified the cause of the lower enzymatic activity of holo‐<I>Ec</I>β<SUB>2</SUB> in comparison with <I>St</I>α<SUB>2</SUB>β<SUB>2</SUB>. The substrate (indole) gate residues, Tyr279 and Phe280, block entry of the substrate into the β<SUB>2</SUB> subunit, although the indole can directly access the active site as a result of a wider cleft between the N and C domains in the holo‐<I>Ec</I>β<SUB>2</SUB> subunit. In addition, the structure around βAsp305 of the holo‐<I>Ec</I>β<SUB>2</SUB> subunit was similar to the open state of <I>St</I>α<SUB>2</SUB>β<SUB>2</SUB> with low activity, resulting in lower activity of holo‐<I>Ec</I>β<SUB>2</SUB>.</P><P><B>Structured digital abstract</B></P><P><P>: <I>Ecβ2</I> (uniprotkb:) and <I>Ecβ2</I> (uniprotkb:) <I>bind </I>() by <I>x‐ray crystallography</I> ()</P><P>: <I>Ecβ2</I> (uniprotkb:) and <I>Ecβ2</I> (uniprotkb:) <I>bind </I>() by <I>biophysical</I> ()</P></P>
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Kim, H. R.,Oh, S. K.,Lee, E. S.,Choi, S. Y.,Roh, S. E.,Kim, S. J.,Tsukihara, T.,Lee, K. Y.,Jeon, C. J.,Kim, U. K. Springer Science + Business Media 2016 HUMAN GENETICS Vol.135 No.3
<P>Gap junctions (GJs) are intercellular channels associated with cell-cell communication. Connexin 26 (Cx26) encoded by the GJB2 gene forms GJs of the inner ear, and mutations of GJB2 cause congenital hearing loss that can be syndromic or non-syndromic. It is difficult to predict pathogenic effects using only genetic analysis. Using ionic and biochemical coupling tests, we evaluated the pathogenic effects of Cx26 variants using computational analyses to predict structural abnormalities. For seven out of ten variants, we predicted the variation would result in a loss of GJ function, whereas the others would completely fail to form GJs. Functional studies demonstrated that, although all variants were able to function normally as hetero-oligomeric GJ channels, six variants (p.E47K, p.E47Q, p.H100L, p.H100Y, p.R127L, and p.M195L) did not function normally as homo-oligomeric GJ channels. Interestingly, GJs composed of the Cx26 variant p.R127H were able to function normally, even as homo-oligomeric GJ channels. This study demonstrates the particular location and property of an amino acid are more important mainly than the domain where they belong in the formation and function of GJ, and will provide information that is useful for the accurate diagnosis of hearing loss.</P>
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A High-Resolution Structure of the Pre-microRNA Nuclear Export Machinery
Okada, Chimari,Yamashita, Eiki,Lee, Soo Jae,Shibata, Satoshi,Katahira, Jun,Nakagawa, Atsushi,Yoneda, Yoshihiro,Tsukihara, Tomitake American Association for the Advancement of Scienc 2009 Science Vol.326 No.5957
<P>Nuclear export of microRNAs (miRNAs) by exportin-5 (Exp-5) is an essential step in miRNA biogenesis. Here, we present the 2.9 angstrom structure of the pre-miRNA nuclear export machinery formed by pre-miRNA complexed with Exp-5 and a guanine triphosphate (GTP)-bound form of the small nuclear guanine triphosphatase (GTPase) Ran (RanGTP). The x-ray structure shows that Exp-5:RanGTP recognizes the 2-nucleotide 3′ overhang structure and the double-stranded stem of the pre-miRNA. Exp-5:RanGTP shields the pre-miRNA stem from degradation in a baseball mitt-like structure where it is held by broadly distributed weak interactions, whereas a tunnel-like structure of Exp-5 interacts strongly with the 2-nucleotide 3′ overhang through hydrogen bonds and ionic interactions. RNA recognition by Exp-5:RanGTP does not depend on RNA sequence, implying that Exp-5:RanGTP can recognize a variety of pre-miRNAs.</P>
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