1ayg: Difference between revisions
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[[Image:1ayg.jpg|left|200px]] | [[Image:1ayg.jpg|left|200px]] | ||
'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1ayg |SIZE=350|CAPTION= <scene name='initialview01'>1ayg</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AYG is a [ | 1AYG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus Hydrogenobacter thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9657676 9657676] | ||
[[Category: Hydrogenobacter thermophilus]] | [[Category: Hydrogenobacter thermophilus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: porphyrin]] | [[Category: porphyrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:53 2008'' | ||
Revision as of 08:03, 20 March 2008
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| Ligands: | HEC | ||||||||||||
| 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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