Crystal structure of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7
-
- OKAI Masahiko
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
-
- KUDO Norio
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
-
- NAGATA Koji
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
-
- LEE Woo Cheol
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
-
- KAMO Masayuki
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
-
- TANOKURA Masaru
- Graduate School of Agricultural and Life Sciences, The University of Tokyo
この論文をさがす
抄録
Flavin reductases (FRs) catalyze the reduction of free flavins using NADH or NADPH. In recent years, a new family of short-chain FRs have been identified in a variety of bacteria and archaea. Here we have determined the crystal structure of an archaeal short-chain FR, HpaC from an aerobic thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7. The HpaC molecule exists as a homodimer with one FMN for each monomer. On the other hand, PheA2, the most structurally similar protein to HpaC, contains FAD rather than FMN. Structural comparison of these proteins has revealed that the short loop at residues 82-83 and the successive η1 helix in HpaC are closer to the bound flavin than those in PheA2. As a result, there is not sufficient space to accommodate the AMP moiety of FAD in HpaC, and thus HpaC prefers FMN to FAD.<br> <br> <br> (Communicated by Masanori OTSUKA, M.J.A.)<br>
収録刊行物
-
- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
-
Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 81 (6), 229-232, 2005
日本学士院
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390282679123340928
-
- NII論文ID
- 130000093802
-
- NII書誌ID
- AA00785485
-
- ISSN
- 13492896
- 03862208
-
- NDL書誌ID
- 7684581
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可