5l89
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Rhodospirillum rubrum Rru_A0973 mutant E32A== | |
| + | <StructureSection load='5l89' size='340' side='right' caption='[[5l89]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5l89]] is a 30 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L89 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5l89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l89 OCA], [http://pdbe.org/5l89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l89 RCSB], [http://www.ebi.ac.uk/pdbsum/5l89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l89 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid. We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface. EncFtn adopts an open decameric structure that is topologically distinct from other ferritins. While EncFtn acts as a ferroxidase, it cannot mineralize iron. Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage. This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins. | ||
| - | + | Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments.,He D, Hughes S, Vanden-Hehir S, Georgiev A, Altenbach K, Tarrant E, Mackay CL, Waldron KJ, Clarke DJ, Marles-Wright J Elife. 2016 Aug 16;5. pii: e18972. doi: 10.7554/eLife.18972. PMID:27529188<ref>PMID:27529188</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5l89" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Altenbach, K]] | [[Category: Altenbach, K]] | ||
| + | [[Category: Clarke, D J]] | ||
[[Category: Georgiev, A]] | [[Category: Georgiev, A]] | ||
[[Category: He, D]] | [[Category: He, D]] | ||
| + | [[Category: Hughes, S]] | ||
| + | [[Category: Mackay, C L]] | ||
| + | [[Category: Marles-Wright, J]] | ||
[[Category: Tarrant, E]] | [[Category: Tarrant, E]] | ||
[[Category: Vanden-Hehir, S]] | [[Category: Vanden-Hehir, S]] | ||
| - | [[Category: | + | [[Category: Waldron, K J]] |
| - | [[Category: | + | [[Category: Ferritin]] |
| - | [[Category: | + | [[Category: Ferroxidase]] |
| - | [[Category: | + | [[Category: Iron oxidation]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
Revision as of 05:04, 9 September 2016
Crystal structure of Rhodospirillum rubrum Rru_A0973 mutant E32A
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