1ayg

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ayg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayg OCA], [http://www.ebi.ac.uk/pdbsum/1ayg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ayg RCSB]</span>
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'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES'''
'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES'''
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[[Category: Yoshida, T.]]
[[Category: Yoshida, T.]]
[[Category: Yu, Y.]]
[[Category: Yu, Y.]]
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[[Category: cytochrome c]]
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[[Category: Cytochrome c]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: ferrous iron]]
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[[Category: Ferrous iron]]
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[[Category: porphyrin]]
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[[Category: Porphyrin]]
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Revision as of 07:50, 2 May 2008

Template:STRUCTURE 1ayg

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. 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 Page seeded by OCA on Fri May 2 10:50:45 2008

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