2019年9月1日
X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein
Acta Crystallographica Section D Structural Biology
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- 巻
- 75
- 号
- 9
- 開始ページ
- 841
- 終了ページ
- 851
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S2059798319010878
- 出版者・発行元
- International Union of Crystallography ({IUCr})
The bacterial flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase complex derived from Burkholderia cepacia (BcGDH) is a representative molecule of direct electron transfer-type FAD-dependent dehydrogenase complexes. In this study, the X-ray structure of BcGDHγα, the catalytic subunit (α-subunit) of BcGDH complexed with a hitchhiker protein (γ-subunit), was determined. The most prominent feature of this enzyme is the presence of the 3Fe-4S cluster, which is located at the surface of the catalytic subunit and functions in intramolecular and intermolecular electron transfer from FAD to the electron-transfer subunit. The structure of the complex revealed that these two molecules are connected through disulfide bonds and hydrophobic interactions, and that the formation of disulfide bonds is required to stabilize the catalytic subunit. The structure of the complex revealed the putative position of the electron-transfer subunit. A comparison of the structures of BcGDHγα and membrane-bound fumarate reductases suggested that the whole BcGDH complex, which also includes the membrane-bound β-subunit containing three heme c moieties, may form a similar overall structure to fumarate reductases, thus accomplishing effective electron transfer.
- リンク情報
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- DOI
- https://doi.org/10.1107/S2059798319010878
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/31478907
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6719666
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000484188400007&DestApp=WOS_CPL
- URL
- http://orcid.org/0000-0003-2136-8042
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85071737262&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85071737262&origin=inward
- ID情報
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- DOI : 10.1107/S2059798319010878
- ISSN : 2059-7983
- eISSN : 2059-7983
- ORCIDのPut Code : 61010450
- PubMed ID : 31478907
- PubMed Central 記事ID : PMC6719666
- SCOPUS ID : 85071737262
- Web of Science ID : WOS:000484188400007