AONO RIKU
Department / Course College of Life Sciences Department of Biotechnology
Title / Position Assistant Professor
Language English
Publication Date 2013/08
Type Research paper (scientific journal)
Peer Review Yes
Title Structure Analysis of Archaeal AMP Phosphorylase Reveals Two Unique Modes of Dimerization
Journal JOURNAL OF MOLECULAR BIOLOGY
Publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Volume, Issue, Page 425(15),2709-2721
Author and coauthor Yuichi Nishitani,Riku Aono,Akira Nakamura,Takaaki Sato,Haruyuki Atomi,Tadayuki Imanaka,Kunio Miki
Details 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 00222836
PMID 23659790
PermalinkURL https://www.sciencedirect.com/science/article/pii/S002228361300274X?via%3Dihub