2018年4月15日
Structure of a [NiFe] hydrogenase maturation protease HycI provides insights into its substrate selectivity
Biochemical and Biophysical Research Communications
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- 巻
- 498
- 号
- 4
- 開始ページ
- 782
- 終了ページ
- 788
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2018.03.058
- 出版者・発行元
- Elsevier B.V.
The immature large subunit of [NiFe] hydrogenases undergoes C-terminal cleavage by a specific protease in the final step of the post-translational process before assembly with other subunits. It has been reported that the [NiFe] hydrogenase maturation protease HycI from Thermococcus kodakarensis (TkHycI) has the catalytic ability to target the membrane-bound hydrogenase large subunit MbhL from T. kodakarensis. However, the detailed mechanism of its substrate recognition remains elusive. We determined the crystal structure of TkHycI at 1.59 Å resolution to clarify how TkHycI recognizes its own substrate MbhL. Although the overall structure of TkHycI is similar to that of its homologous protease TkHybD, TkHycI adopts a larger loop than TkHybD, thereby creating a broad and deep cleft. We analyzed the structural properties of the TkHycI cleft probably involved in its substrate recognition. Our findings provide novel and profound insights into the substrate selectivity of TkHycI.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.bbrc.2018.03.058
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/29526754
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000430158200013&DestApp=WOS_CPL
- URL
- http://orcid.org/0000-0003-3537-2114
- ID情報
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- DOI : 10.1016/j.bbrc.2018.03.058
- ISSN : 1090-2104
- ISSN : 0006-291X
- ORCIDのPut Code : 42679527
- PubMed ID : 29526754
- SCOPUS ID : 85044143374
- Web of Science ID : WOS:000430158200013