1ayg
From Proteopedia
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SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1AYG is a Single protein structure of sequence from Hydrogenobacter thermophilus with HEC as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy., Hasegawa J, Yoshida T, Yamazaki T, Sambongi Y, Yu Y, Igarashi Y, Kodama T, Yamazaki K, Kyogoku Y, Kobayashi Y, Biochemistry. 1998 Jul 7;37(27):9641-9. PMID:9657676
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