アオノ リク
青野 陸
AONO RIKU
所属 生命科学部 生物工学科
職名 助教
言語種別 英語
発行・発表の年月 2013/08
形態種別 研究論文(学術雑誌)
査読 査読あり
標題 Structure Analysis of Archaeal AMP Phosphorylase Reveals Two Unique Modes of Dimerization
執筆形態 不明
掲載誌名 JOURNAL OF MOLECULAR BIOLOGY
出版社・発行元 ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
巻・号・頁 425(15),2709-2721
著者・共著者 Yuichi Nishitani,Riku Aono,Akira Nakamura,Takaaki Sato,Haruyuki Atomi,Tadayuki Imanaka,Kunio Miki
概要 AMP phosphorylase (AMPpase) catalyzes the initial reaction in a novel AMP metabolic pathway recently found in archaea, converting AMP and phosphate into adenine and ribose 1,5-bisphosphate. Gel-filtration chromatography revealed that AMPpase from Thermococcus kodakarensis (Tk-AMPpase) forms an exceptionally large macromolecular structure (>40-mers) in solution. To investigate its unique multimerization feature, we determined the first crystal structures of Tk-AMPpase, in the apo-form and in complex with substrates. Structures of two truncated forms of Tk-AMPpase (Tk-AMPpase Delta N84 and Tk-AMPpase Delta C10) clarified that this multimerization is achieved by two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain, which consists of an unexpected domain-swapping interaction. The N-terminal domain, characteristic of archaeal enzymes, is essential for enzymatic activity, participating in nnultimerization as well as domain closure of the active site upon substrate binding. Moreover, biochemical analysis demonstrated that the macromolecular assembly of Tk-AMPpase contributes to its high thermostability, essential for an enzyme from a hyperthermophile. Our findings unveil a unique archaeal nucleotide phosphorylase that is distinct in both function and structure from previously known members of the nucleoside phosphorylase II family. (C) 2013 Elsevier Ltd. All rights reserved.
DOI 10.1016/j.jmb.2013.04.026
ISSNコード 00222836
PMID 23659790
PermalinkURL https://www.sciencedirect.com/science/article/pii/S002228361300274X?via%3Dihub