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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2015/12 |
| 形態種別 | 研究論文 |
| 標題 | Conformational plasticity is crucial for C3-RhoA complex formation by ARTT-loop. |
| 執筆形態 | その他 |
| 掲載誌名 | PATHOGENS AND DISEASE |
| 出版社・発行元 | OXFORD UNIV PRESS |
| 巻・号・頁 | 73(9) |
| 担当区分 | 筆頭著者,責任著者 |
| 著者・共著者 | Tsuge H,Yoshida T,Tsurumura T |
| 概要 | ADP-ribosylation is an important post-translational protein modification catalyzed by bacterial toxins and eukaryotic endogenous ADP-ribosyltransferases. Bacterial binary toxins and C3-like toxins recognize and ADP-ribosylate actin Arg177 and RhoA Asn41, respectively. Structural and mutational studies have identified an ADP-ribosylating turn-turn loop (ARTT-loop) that has been implicated in substrate specificity and recognition, although it has not been verified. Recently, we determined the crystal structure of the C3 exoenzyme-RhoA complex. The complex structure shows how C3 recognizes Rho GTPase and provides the first structural evidence for RhoA recognition by the ARTT-loop. The complex formation mediated by the ARTT-loop is through the intrinsic plasticity of C3 and RhoA. C3 changes the conformations of both the phosphate nicotinamide-loop and the ARTT-loop by NAD(+) and RhoA binding, respectively. In contrast, RhoA changes the conformations of switch I and II regions upon C3 binding with a particular conformation, irrespective of the bound nucleotide (GTP or GDP). |
| DOI | 10.1093/femspd/ftv094 |
| ISSN | 2049-632X |
| PMID | 26474844 |
| Put Code(ORCID) | 26473844 |
| PermalinkURL | http://europepmc.org/abstract/med/26474844 |