1AYG
SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
1AYG の概要
| エントリーDOI | 10.2210/pdb1ayg/pdb |
| NMR情報 | BMRB: 5086 |
| 分子名称 | CYTOCHROME C-552, HEME C (2 entities in total) |
| 機能のキーワード | cytochrome c, electron transport, porphyrin, ferrous iron |
| 由来する生物種 | Hydrogenobacter thermophilus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9204.52 |
| 構造登録者 | Hasegawa, J.,Yoshida, T.,Yamazaki, T.,Sambongi, Y.,Yu, Y.,Igarashi, Y.,Kodama, T.,Yamazaki, K.,Hakusui, H.,Kyogoku, Y.,Kobayashi, Y. (登録日: 1997-11-04, 公開日: 1998-11-25, 最終更新日: 2024-10-09) |
| 主引用文献 | Hasegawa, J.,Yoshida, T.,Yamazaki, T.,Sambongi, Y.,Yu, Y.,Igarashi, Y.,Kodama, T.,Yamazaki, K.,Kyogoku, Y.,Kobayashi, Y. Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy. Biochemistry, 37:9641-9649, 1998 Cited by PubMed Abstract: The solution structure of a thermostable cytochrome c-552 from a thermophilic hydrogen oxidizing bacterium Hydrogenobacter thermophilus was determined by proton nuclear magnetic resonance spectroscopy. Twenty structures were calculated by the X-PLOR program on the basis of 902 interproton distances, 21 hydrogen bonds, and 13 torsion angle constraints. The pairwise average root-mean-square deviation for the main chain heavy atoms was 0.91 +/- 0.11 A. The main chain folding of the cytochrome c-552 was almost the same as that of Pseudomonas aeruginosa cytochrome c-551 that has 59% sequence identity to the cytochrome c-552 but is less thermostable. We found several differences in local structures between the cytochromes c-552 and c-551. In the cytochrome c-552, aromatic-amino interactions were uniquely formed between Arg 35 and Tyr 32 and/or Tyr 41, the latter also having hydrophobic contacts with the side chains of Tyr 32, Ala 38, and Leu 42. Small hydrophobic cores were more tightly packed in the cytochrome c-552 because of the occupancies of Ala 5, Met 11, and Ile 76, each substituted by Phe 7, Val 13, and Val 78, respectively, in the cytochrome c-551. Some of these structural differences may contribute to the higher thermostability of the cytochrome c-552. PubMed: 9657676DOI: 10.1021/bi9803067 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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