6s6c: Difference between revisions
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==Ground state structure of Archaerhodopsin-3 at 100K== | ==Ground state structure of Archaerhodopsin-3 at 100K== | ||
<StructureSection load='6s6c' size='340' side='right'caption='[[6s6c]]' scene=''> | <StructureSection load='6s6c' size='340' side='right'caption='[[6s6c]], [[Resolution|resolution]] 1.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S6C OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6s6c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorubrum_sodomense Halorubrum sodomense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S6C FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.07Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=R16:HEXADECANE'>R16</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=6s6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s6c OCA], [https://pdbe.org/6s6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s6c RCSB], [https://www.ebi.ac.uk/pdbsum/6s6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s6c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BACR3_HALSD BACR3_HALSD] Light-driven proton pump. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in the prolonged absence of light. Here, we present high-resolution crystal structures of the ground (light-adapted) and DA states of Archaerhodopsin-3 (AR3), solved to 1.1 A and 1.3 A resolution respectively. We observe significant differences between the two states in the dynamics of water molecules that are coupled via H-bonds to the retinal Schiff Base. Supporting QM/MM calculations reveal how the DA state permits a thermodynamic equilibrium between retinal isomers to be established, and how this same change is prevented in the ground state in the absence of light. We suggest that the different arrangement of internal water networks in AR3 is responsible for the faster photocycle kinetics compared to homologs. | |||
Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.,Bada Juarez JF, Judge PJ, Adam S, Axford D, Vinals J, Birch J, Kwan TOC, Hoi KK, Yen HY, Vial A, Milhiet PE, Robinson CV, Schapiro I, Moraes I, Watts A Nat Commun. 2021 Jan 27;12(1):629. doi: 10.1038/s41467-020-20596-0. PMID:33504778<ref>PMID:33504778</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6s6c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Halorubrum sodomense]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Axford D]] | [[Category: Axford D]] | ||
Revision as of 15:36, 24 January 2024
Ground state structure of Archaerhodopsin-3 at 100KGround state structure of Archaerhodopsin-3 at 100K
Structural highlights
FunctionBACR3_HALSD Light-driven proton pump. Publication Abstract from PubMedMany transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in the prolonged absence of light. Here, we present high-resolution crystal structures of the ground (light-adapted) and DA states of Archaerhodopsin-3 (AR3), solved to 1.1 A and 1.3 A resolution respectively. We observe significant differences between the two states in the dynamics of water molecules that are coupled via H-bonds to the retinal Schiff Base. Supporting QM/MM calculations reveal how the DA state permits a thermodynamic equilibrium between retinal isomers to be established, and how this same change is prevented in the ground state in the absence of light. We suggest that the different arrangement of internal water networks in AR3 is responsible for the faster photocycle kinetics compared to homologs. Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.,Bada Juarez JF, Judge PJ, Adam S, Axford D, Vinals J, Birch J, Kwan TOC, Hoi KK, Yen HY, Vial A, Milhiet PE, Robinson CV, Schapiro I, Moraes I, Watts A Nat Commun. 2021 Jan 27;12(1):629. doi: 10.1038/s41467-020-20596-0. PMID:33504778[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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