1ayg

<StructureSection load='1ayg' size='340' side='right' caption='[[1ayg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ayg]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AYG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[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://pdbe.org/1ayg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ayg RCSB], [http://www.ebi.ac.uk/pdbsum/1ayg PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CY552_HYDTT CY552_HYDTT]] Reacts with hydrogenase.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/1ayg_consurf.spt"</scriptWhenChecked>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ayg" style="background-color:#fffaf0;"></div>

*[[Nitric reductase|Nitric reductase]]

[[Category: Hakusui, H]]

[[Category: Hasegawa, J]]

[[Category: Igarashi, Y]]

[[Category: Kobayashi, Y]]

[[Category: Kodama, T]]

[[Category: Kyogoku, Y]]

[[Category: Sambongi, Y]]

[[Category: Yamazaki, K]]

[[Category: Yamazaki, T]]

[[Category: Yoshida, T]]

[[Category: Yu, Y]]

[[Category: Porphyrin]]