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인간의 c - Ha - ras 발암성 단백질에 결합되어 있는 GDP 와 GTPγ의 형태 비교
하종명,Gota Kawai,Tatsuo Miyazawa,Shigeyuki Yokoyama ( Jong Myung Ha ) 생화학분자생물학회 1993 BMB Reports Vol.26 No.1
A normal ras protein and two of the mutant proteins were prepared to investigate the biochemical properties of ras proteins produced by ras genes. The methods for the preparation of ras proteins include 1) the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal producing [ras(G12/1-171) protein], 2) the replacement of glycine by valine at position 12 of the ras protein from amino-terminal followed by the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal [ras(V12/1-171) protein], 3) the replacement of glutamine by leucine at the position 61 followed by the truncation of c-Ha-ras protein at the position 18 from carboxy-terminal [ras(L61/1-171) protein]. The proton resonances of H8(guanine) and H1`, H2`, H3`, H4`, H5` (ribose) of the GDP and the GTP_γS [Guanosine 5`-0-(3-thiotriphosphate)] bound to ras(1-171) proteins were identified. By numerical simulation of these irradiated time-dependent NOE profiles, the conformations of the protein-bound GDP and GTP S were elucidated. The guanosine moieties of GDPs bound to three ras(1-171) proteins take the anti form about the N-glycosidic bond with a dihedral angle of χ= -120° and the ribose ring take the C2`-endo forms that were independent with point mutation. In contrast to the conformation of the bound GDP, the guanosine moieties of GTP_γSs bound to ras(1-171) proteins had anti-C3`-endo form and a dihedral angle of χ=-80°, and were not affected by the point mutation of ras(1-171) protein. The role of the interaction between the bound guanine nucleotide and effector region is discussed with regard to the mechanism of the ras proteins.
Kikukawa, Takashi,Shimono, Kazumi,Tamogami, Jun,Miyauchi, Seiji,Kim, So Young,Kimura-Someya, Tomomi,Shirouzu, Mikako,Jung, Kwang-Hwan,Yokoyama, Shigeyuki,Kamo, Naoki American ChemicalSociety 2011 Biochemistry Vol.50 No.41
<P><I>Acetabularia</I> rhodopsins are the firstmicrobialrhodopsins discovered in a marine plant organism, <I>Acetabulariaacetabulum</I>. Previously, we expressed <I>Acetabularia</I> rhodopsin II (ARII) by a cell-free system from one of two opsingenes in <I>A. acetabulum</I> cDNA and showed that ARIIis a light-driven proton pump [Wada, T., et al. (2011) <I>J.Mol. Biol.</I><I>411</I>, 986–998]. In thisstudy, the photochemistry of ARII was examined using the flash-photolysistechnique, and data were analyzed using a sequential irreversiblemodel. Five photochemically defined intermediates (P<SUB><I>i</I></SUB>) were sufficient to simulate the data. Noticeably, both P<SUB>3</SUB> and P<SUB>4</SUB> contain an equilibrium mixture of M, N,and O. Using a transparent indium tin oxide electrode, the photoinducedproton transfer was measured over a wide pH range. Analysis of thepH-dependent proton transfer allowed estimation of the p<I>K</I><SUB>a</SUB> values of some amino acid residues. The estimated valueswere 2.6, 5.9 (or 6.3), 8.4, 9.3, 10.5, and 11.3. These values wereassigned as the p<I>K</I><SUB>a</SUB> of Asp81 (Asp85<SUP>BR</SUP>) in the dark, Asp92 (Asp96<SUP>BR</SUP>) at N, Glu199 (Glu204<SUP>BR</SUP>) at M, Glu199 in the dark, an undetermined proton-releasingresidue at the release, and the pH to start denaturation, respectively.Following this analysis, the proton transfer of ARII is discussed.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/2011/bichaw.2011.50.issue-41/bi2009932/production/images/medium/bi-2011-009932_0006.gif'></P>
High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26.
Won, Eun Young,Xie, Yong,Takemoto, Chie,Chen, Lirong,Liu, Zhi Jie,Wang, Bi Cheng,Lee, Daeyoup,Woo, Eui Jeon,Park, Sung Goo,Shirouzu, Mikako,Yokoyama, Shigeyuki,Kim, Seung Jun,Chi, Seung Wook Wiley-Blackwell 2013 Acta crystallographica. Section D, Biological crys Vol.69 No.6
<P>Dual-specificity phosphatases (DUSPs) play an important role in regulating cellular signalling pathways governing cell growth, differentiation and apoptosis. Human DUSP26 inhibits the apoptosis of cancer cells by dephosphorylating substrates such as p38 and p53. High-resolution crystal structures of the DUSP26 catalytic domain (DUSP26-C) and its C152S mutant [DUSP26-C (C152S)] have been determined at 1.67 and 2.20 ? resolution, respectively. The structure of DUSP26-C showed a novel type of domain-swapped dimer formed by extensive crossover of the C-terminal α7 helix. Taken together with the results of a phosphatase-activity assay, structural comparison with other DUSPs revealed that DUSP26-C adopts a catalytically inactive conformation of the protein tyrosine phosphate-binding loop which significantly deviates from that of canonical DUSP structures. In particular, a noticeable difference exists between DUSP26-C and the active forms of other DUSPs at the hinge region of a swapped C-terminal domain. Additionally, two significant gaps were identified between the catalytic core and its surrounding loops in DUSP26-C, which can be exploited as additional binding sites for allosteric enzyme regulation. The high-resolution structure of DUSP26-C may thus provide structural insights into the rational design of DUSP26-targeted anticancer drugs.</P>