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| | <StructureSection load='4cyb' size='340' side='right'caption='[[4cyb]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='4cyb' size='340' side='right'caption='[[4cyb]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cyb]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CYB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cyb]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CYB 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cy9|4cy9]], [[4cya|4cya]]</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4cyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyb OCA], [http://pdbe.org/4cyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cyb RCSB], [http://www.ebi.ac.uk/pdbsum/4cyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyb 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=4cyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyb OCA], [https://pdbe.org/4cyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cyb RCSB], [https://www.ebi.ac.uk/pdbsum/4cyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9K3L0_STRCO Q9K3L0_STRCO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hitchings, M D]] | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Pohl, E]]
| + | [[Category: Del Sol R]] |
| - | [[Category: Sol, R Del]] | + | [[Category: Hitchings MD]] |
| - | [[Category: Townsend, P D]] | + | [[Category: Pohl E]] |
| - | [[Category: Dp]] | + | [[Category: Townsend PD]] |
| - | [[Category: Ferritin]] | + | |
| - | [[Category: Iron binding protein]]
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| Structural highlights
Function
Q9K3L0_STRCO
Publication Abstract from PubMed
Dps proteins are members of an extensive family of proteins that oxidise and deposit iron in the form of ferric oxide, and are also able to bind DNA. Ferroxidation centres are formed at the interface of anti-parallel dimers, which further assemble into dodecameric nanocages with a hollow core where ferric oxide is deposited. Streptomyces coelicolor encodes three Dps-like proteins (DpsA, B and C). Despite sharing the conserved four-helix bundle organisation observed in members of the Dps family, they display significant differences in the length of terminal extensions, or tails. DpsA possess both N- and C-terminal tails of different lengths, and their removal affects quaternary structure assembly to varying degrees. DpsC quaternary structure, on the other hand, is heavily dependent on its N-terminal tail as its removal abolishes correct protein folding. Analysis of the crystal structure of dodecamers from both proteins revealed remarkable differences in the position of tails and interface surface area; and provides insight to explain the differences in biochemical behaviour observed while comparing DpsA and DpsC.
A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor.,Hitchings MD, Townsend P, Pohl E, Facey PD, Jones DH, Dyson PJ, Del Sol R Cell Mol Life Sci. 2014 Jun 11. PMID:24915944[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hitchings MD, Townsend P, Pohl E, Facey PD, Jones DH, Dyson PJ, Del Sol R. A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor. Cell Mol Life Sci. 2014 Jun 11. PMID:24915944 doi:http://dx.doi.org/10.1007/s00018-014-1658-4
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