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1ayg

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[[Image:1ayg.jpg|left|200px]]<br /><applet load="1ayg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ayg" />
 
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'''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES==
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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.
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<StructureSection load='1ayg' size='340' side='right'caption='[[1ayg]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CY552_HYDTT CY552_HYDTT] Reacts with hydrogenase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AYG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus Hydrogenobacter thermophilus] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYG OCA].
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*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9657676 9657676]
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[[Category: Hydrogenobacter thermophilus]]
[[Category: Hydrogenobacter thermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hakusui, H.]]
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[[Category: Hakusui H]]
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[[Category: Hasegawa, J.]]
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[[Category: Hasegawa J]]
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[[Category: Igarashi, Y.]]
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[[Category: Igarashi Y]]
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[[Category: Kobayashi, Y.]]
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[[Category: Kobayashi Y]]
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[[Category: Kodama, T.]]
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[[Category: Kodama T]]
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[[Category: Kyogoku, Y.]]
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[[Category: Kyogoku Y]]
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[[Category: Sambongi, Y.]]
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[[Category: Sambongi Y]]
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[[Category: Yamazaki, K.]]
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[[Category: Yamazaki K]]
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[[Category: Yamazaki, T.]]
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[[Category: Yamazaki T]]
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[[Category: Yoshida, T.]]
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[[Category: Yoshida T]]
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[[Category: Yu, Y.]]
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[[Category: Yu Y]]
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[[Category: HEC]]
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[[Category: cytochrome c]]
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[[Category: electron transport]]
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[[Category: ferrous iron]]
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[[Category: porphyrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:39 2008''
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Current revision

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

PDB ID 1ayg

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