2007年3月9日
Structure of Thiocyanate Hydrolase: A New Nitrile Hydratase Family Protein with a Novel Five-coordinate Cobalt(III) Center
Journal of Molecular Biology
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- 巻
- 366
- 号
- 5
- 開始ページ
- 1497
- 終了ページ
- 1509
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.jmb.2006.12.011
- 出版者・発行元
- ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Thiocyanate hydrolase (SCNase) of Thiobacillus thioparus THI115 is a cobalt(III)-containing enzyme catalyzing the degradation of thiocyanate to carbonyl sulfide and ammonia. We determined the crystal structures of the apo- and native SCNases at a resolution of 2.0 Å. SCNases in both forms had a conserved hetero-dodecameric structure, (αβγ)4. Four αβγ hetero-trimers were structurally equivalent. One αβγ hetero-trimer was composed of the core domain and the βN domain, which was located at the center of the molecule and linked the hetero-trimers with novel quaternary interfaces. In both the apo- and native SCNases, the core domain was structurally conserved between those of iron and cobalt-types of nitrile hydratase (NHase). Native SCNase possessed the post-translationally modified cysteine ligands, γCys131-SO2H and γCys133-SOH like NHases. However, the low-spin cobalt(III) was found to be in the distorted square-pyramidal geometry, which had not been reported before in any protein. The size as well as the electrostatic properties of the substrate-binding pocket was totally different from NHases with respect to the charge distribution and the substrate accessibility, which rationally explains the differences in the substrate preference between SCNase and NHase. © 2006 Elsevier Ltd. All rights reserved.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.jmb.2006.12.011
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/17222425
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000244621100011&DestApp=WOS_CPL
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33846799140&origin=inward
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=33846799140&origin=inward
- URL
- http://orcid.org/0000-0001-6496-5440
- ID情報
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- DOI : 10.1016/j.jmb.2006.12.011
- ISSN : 0022-2836
- eISSN : 1089-8638
- ORCIDのPut Code : 32468768
- PubMed ID : 17222425
- SCOPUS ID : 33846799140
- Web of Science ID : WOS:000244621100011