5aur: Difference between revisions
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New page: '''Unreleased structure''' The entry 5aur is ON HOLD Authors: Ren, C., Nagao, S., Yamanaka, M., Kamikubo, H., Komori, H., Shomura, Y., Higuchi, Y., Hirota, S. Description: Hydrogenobac... |
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==Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region== | |||
<StructureSection load='5aur' size='340' side='right'caption='[[5aur]], [[Resolution|resolution]] 1.26Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5aur]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydrogenobacter_thermophilus_TK-6 Hydrogenobacter thermophilus TK-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AUR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.26Å</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>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=5aur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aur OCA], [https://pdbe.org/5aur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aur RCSB], [https://www.ebi.ac.uk/pdbsum/5aur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aur ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CY552_HYDTT CY552_HYDTT] Reacts with hydrogenase. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
High-order oligomers of Hydrogenobacter thermophilus cytochrome c552 increased with the insertion of more Gly residues between Ala18 and Lys19 at the major hinge loop of the wild-type protein. N-Terminal domain swapping and C-terminal domain swapping were elucidated by using X-ray crystallography for the mutant with the insertion of three Gly residues at the hinge loop. | |||
Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome cvia the elongation of the major hinge loop.,Ren C, Nagao S, Yamanaka M, Komori H, Shomura Y, Higuchi Y, Hirota S Mol Biosyst. 2015 Oct 9. PMID:26451671<ref>PMID:26451671</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hirota | <div class="pdbe-citations 5aur" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Nagao | __TOC__ | ||
[[Category: Ren | </StructureSection> | ||
[[Category: Shomura | [[Category: Hydrogenobacter thermophilus TK-6]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Higuchi Y]] | |||
[[Category: Hirota S]] | |||
[[Category: Kamikubo H]] | |||
[[Category: Komori H]] | |||
[[Category: Nagao S]] | |||
[[Category: Ren C]] | |||
[[Category: Shomura Y]] | |||
[[Category: Yamanaka M]] | |||
Latest revision as of 15:48, 8 November 2023
Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region
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