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| | <StructureSection load='4cmy' size='340' side='right'caption='[[4cmy]], [[Resolution|resolution]] 2.59Å' scene=''> | | <StructureSection load='4cmy' size='340' side='right'caption='[[4cmy]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cmy]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49652 Atcc 49652]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cmy]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum Chlorobaculum tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CMY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=4cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmy OCA], [http://pdbe.org/4cmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cmy RCSB], [http://www.ebi.ac.uk/pdbsum/4cmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cmy ProSAT]</span></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=4cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmy OCA], [https://pdbe.org/4cmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cmy RCSB], [https://www.ebi.ac.uk/pdbsum/4cmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cmy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q8KBP5_CHLTE Q8KBP5_CHLTE]] Iron storage protein.[RuleBase:RU361145] | + | [[https://www.uniprot.org/uniprot/Q8KBP5_CHLTE Q8KBP5_CHLTE]] Iron storage protein.[RuleBase:RU361145] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ferritin|Ferritin]] | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49652]] | + | [[Category: Chlorobaculum tepidum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arenas, M]] | + | [[Category: Arenas M]] |
| - | [[Category: Pohl, E]] | + | [[Category: Pohl E]] |
| - | [[Category: Townsend, P D]] | + | [[Category: Townsend PD]] |
| - | [[Category: Yevenes, A]] | + | [[Category: Yevenes A]] |
| - | [[Category: Iron metabolism]]
| + | |
| - | [[Category: Iron-storage protein]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| Structural highlights
Function
[Q8KBP5_CHLTE] Iron storage protein.[RuleBase:RU361145]
Publication Abstract from PubMed
Ferritins are ubiquitous iron-storage proteins found in all kingdoms of life. They share a common architecture made of 24 subunits of five alpha-helices. The recombinant Chlorobium tepidum ferritin (rCtFtn) is a structurally interesting protein since sequence alignments with other ferritins show that this protein has a significantly extended C-terminus, which possesses 12 histidine residues as well as several aspartate and glutamic acid residues that are potential metal ion binding residues. We show that the macromolecular assembly of rCtFtn exhibits a cage-like hollow shell consisting of 24 monomers that are related by 4-3-2 symmetry; similar to the assembly of other ferritins. In all ferritins of known structure the short fifth alpha-helix adopts an acute angle with respect to the four-helix bundle. However, the crystal structure of the rCtFtn presented here shows that this helix adopts a new conformation defining a new assembly of the 4-fold channel of rCtFtn. This conformation allows the arrangement of the C-terminal region into the inner cavity of the protein shell. Furthermore, two Fe(III) ions were found in each ferroxidase center of rCtFtn, with an average FeA-FeB distance of 3 A; corresponding to a diferric mu-oxo/hydroxo species. This is the first ferritin crystal structure with an isolated di-iron center in an iron-storage ferritin. The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.
The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family.,Arenas-Salinas M, Townsend PD, Brito C, Marquez V, Marabolli V, Gonzalez-Nilo F, Matias C, Watt RK, Lopez-Castro JD, Dominguez-Vera J, Pohl E, Yevenes A Biochimie. 2014 Nov;106:39-47. doi: 10.1016/j.biochi.2014.07.019. Epub 2014 Jul, 28. PMID:25079050[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arenas-Salinas M, Townsend PD, Brito C, Marquez V, Marabolli V, Gonzalez-Nilo F, Matias C, Watt RK, Lopez-Castro JD, Dominguez-Vera J, Pohl E, Yevenes A. The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family. Biochimie. 2014 Nov;106:39-47. doi: 10.1016/j.biochi.2014.07.019. Epub 2014 Jul, 28. PMID:25079050 doi:http://dx.doi.org/10.1016/j.biochi.2014.07.019
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