8aca: Difference between revisions
New page: '''Unreleased structure''' The entry 8aca is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==SDBC DR_0644 subunit, only-Cu Superoxide Dismutase== | ||
<StructureSection load='8aca' size='340' side='right'caption='[[8aca]], [[Resolution|resolution]] 2.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8aca]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ACA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ACA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.54Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=8aca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aca OCA], [https://pdbe.org/8aca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aca RCSB], [https://www.ebi.ac.uk/pdbsum/8aca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aca ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RWM2_DEIRA Q9RWM2_DEIRA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu-only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for approximately 280 A, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evolutive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies. | |||
The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans.,Farci D, Graca AT, Iesu L, de Sanctis D, Piano D J Biol Chem. 2023 Jan;299(1):102784. doi: 10.1016/j.jbc.2022.102784. Epub 2022 , Dec 9. PMID:36502921<ref>PMID:36502921</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8aca" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Deinococcus radiodurans R1]] | |||
[[Category: Large Structures]] | |||
[[Category: Farci D]] | |||
[[Category: Piano D]] | |||
Latest revision as of 09:44, 24 July 2024
SDBC DR_0644 subunit, only-Cu Superoxide DismutaseSDBC DR_0644 subunit, only-Cu Superoxide Dismutase
Structural highlights
FunctionPublication Abstract from PubMedDeinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu-only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for approximately 280 A, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evolutive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies. The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans.,Farci D, Graca AT, Iesu L, de Sanctis D, Piano D J Biol Chem. 2023 Jan;299(1):102784. doi: 10.1016/j.jbc.2022.102784. Epub 2022 , Dec 9. PMID:36502921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||