1ayg
From Proteopedia
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|PDB= 1ayg |SIZE=350|CAPTION= <scene name='initialview01'>1ayg</scene> | |PDB= 1ayg |SIZE=350|CAPTION= <scene name='initialview01'>1ayg</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Yoshida, T.]] | [[Category: Yoshida, T.]] | ||
[[Category: Yu, Y.]] | [[Category: Yu, Y.]] | ||
| - | [[Category: HEC]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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[[Category: porphyrin]] | [[Category: porphyrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:04 2008'' |
Revision as of 15:50, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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