1AYG

SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES

Summary for 1AYG

• Entry DOI: 10.2210/pdb1ayg/pdb
• NMR Information: BMRB: 5086
• Descriptor: CYTOCHROME C-552, HEME C (2 entities in total)
• Functional Keywords: cytochrome c, electron transport, porphyrin, ferrous iron
• Biological source: Hydrogenobacter thermophilus
• Total number of polymer chains: 1
• Total formula weight: 9204.52

Authors

Hasegawa, J.,Yoshida, T.,Yamazaki, T.,Sambongi, Y.,Yu, Y.,Igarashi, Y.,Kodama, T.,Yamazaki, K.,Hakusui, H.,Kyogoku, Y.,Kobayashi, Y. (deposition date: 1997-11-04, release date: 1998-11-25, Last modification date: 2024-10-09)

Primary citation

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

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: 9657676
DOI: 10.1021/bi9803067

Experimental method

SOLUTION NMR