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[[Image:1ayg.jpg|left|200px]]
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{{STRUCTURE_1ayg|  PDB=1ayg  |  SCENE=  }}
'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES'''


==SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES==
<StructureSection load='1ayg' size='340' side='right'caption='[[1ayg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ayg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus Hydrogenobacter thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AYG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ayg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayg OCA], [https://pdbe.org/1ayg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ayg RCSB], [https://www.ebi.ac.uk/pdbsum/1ayg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ayg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CY552_HYDTT CY552_HYDTT] Reacts with hydrogenase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ayg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:9657676</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1ayg" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hydrogenobacter thermophilus]]
[[Category: Hydrogenobacter thermophilus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hakusui, H.]]
[[Category: Hakusui H]]
[[Category: Hasegawa, J.]]
[[Category: Hasegawa J]]
[[Category: Igarashi, Y.]]
[[Category: Igarashi Y]]
[[Category: Kobayashi, Y.]]
[[Category: Kobayashi Y]]
[[Category: Kodama, T.]]
[[Category: Kodama T]]
[[Category: Kyogoku, Y.]]
[[Category: Kyogoku Y]]
[[Category: Sambongi, Y.]]
[[Category: Sambongi Y]]
[[Category: Yamazaki, K.]]
[[Category: Yamazaki K]]
[[Category: Yamazaki, T.]]
[[Category: Yamazaki T]]
[[Category: Yoshida, T.]]
[[Category: Yoshida T]]
[[Category: Yu, Y.]]
[[Category: Yu Y]]
[[Category: Cytochrome c]]
[[Category: Electron transport]]
[[Category: Ferrous iron]]
[[Category: Porphyrin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:50:45 2008''

Latest revision as of 05:25, 13 August 2026

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

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