1ayg: Difference between revisions
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New page: left|200px<br /><applet load="1ayg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayg" /> '''SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR,... |
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== | ==SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES== | ||
The solution structure of a thermostable cytochrome c-552 from a | <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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ayg" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hydrogenobacter thermophilus]] | [[Category: Hydrogenobacter thermophilus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hakusui | [[Category: Hakusui H]] | ||
[[Category: Hasegawa | [[Category: Hasegawa J]] | ||
[[Category: Igarashi | [[Category: Igarashi Y]] | ||
[[Category: Kobayashi | [[Category: Kobayashi Y]] | ||
[[Category: Kodama | [[Category: Kodama T]] | ||
[[Category: Kyogoku | [[Category: Kyogoku Y]] | ||
[[Category: Sambongi | [[Category: Sambongi Y]] | ||
[[Category: Yamazaki | [[Category: Yamazaki K]] | ||
[[Category: Yamazaki | [[Category: Yamazaki T]] | ||
[[Category: Yoshida | [[Category: Yoshida T]] | ||
[[Category: Yu | [[Category: Yu Y]] | ||
