5aus
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at C-terminal region== |
+ | <StructureSection load='5aus' size='340' side='right' caption='[[5aus]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5aus]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AUS 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vym|3vym]], [[5aur|5aur]]</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=5aus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aus OCA], [http://pdbe.org/5aus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aus RCSB], [http://www.ebi.ac.uk/pdbsum/5aus PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://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> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 5aus" style="background-color:#fffaf0;"></div> | |
- | [[Category: | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Higuchi, Y]] | ||
[[Category: Hirota, S]] | [[Category: Hirota, S]] | ||
- | [[Category: | + | [[Category: Komori, H]] |
- | + | ||
[[Category: Nagao, S]] | [[Category: Nagao, S]] | ||
[[Category: Ren, C]] | [[Category: Ren, C]] | ||
[[Category: Shomura, Y]] | [[Category: Shomura, Y]] | ||
- | [[Category: | + | [[Category: Yamanaka, M]] |
+ | [[Category: Electron transport]] |
Revision as of 05:23, 22 October 2015
Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at C-terminal region
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Categories: Higuchi, Y | Hirota, S | Komori, H | Nagao, S | Ren, C | Shomura, Y | Yamanaka, M | Electron transport