2015年5月
Open-close structural change upon ligand binding and two magnesium ions required for the catalysis of N-acetylhexosamine 1-kinase
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
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- 巻
- 1854
- 号
- 5
- 開始ページ
- 333
- 終了ページ
- 340
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbapap.2015.01.011
- 出版者・発行元
- ELSEVIER SCIENCE BV
Infant gut-associated bifidobacteria possess a metabolic pathway to utilize lacto-N-biose (Gal-beta 1,3-G1cNAc) and galacto-N-biose (Gal-beta 1,3-GalNAc) from human milk and glycoconjugates specifically. In this pathway, N-acetylhexosamine 1-kinase (NahK) catalyzes the phosphorylation of GlcNAc or GalNAc at the anomeric Cl position with ATP. Crystal structures of NahK have only been determined in the closed state. In this study, we determined open state structures of NahK in three different forms (apo, ADP complex, and ATP complex). A comparison of the open and closed state structures revealed an induced fit structural change defined by two rigid domains. ATP binds to the small N-terminal domain, and binding of the N-acetylhexosamine substrate to the large C-terminal domain induces a closing conformational change with a rotation angle of 16 degrees. In the nucleotide binding site, two magnesium ions bridging the alpha-gamma and beta-gamma phosphates were identified. A mutational analysis indicated that a residue coordinating both of the two magnesium ions (Asp228) is essential for catalysis. The involvement of two magnesium ions in the catalytic machinery is structurally similar to the catalytic structures of protein kinases and aminoglycoside phosphotransferases, but distinct from the structures of other anomeric kinases or sugar 6-kinases. These findings help to elucidate the possible evolutionary adaptation of substrate specificities and induced fit mechanism. (C) 2015 Elsevier B.V. All rights reserved.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.bbapap.2015.01.011
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/25644306
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000353089600003&DestApp=WOS_CPL
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84922470089&origin=inward
- ID情報
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- DOI : 10.1016/j.bbapap.2015.01.011
- ISSN : 1570-9639
- eISSN : 0006-3002
- PubMed ID : 25644306
- SCOPUS ID : 84922470089
- Web of Science ID : WOS:000353089600003