4ar5: Difference between revisions
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<StructureSection load='4ar5' size='340' side='right'caption='[[4ar5]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='4ar5' size='340' side='right'caption='[[4ar5]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ar5]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ar5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AR5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <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=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bq8|1bq8]], [[1bq9|1bq9]], [[1brf|1brf]], [[1caa|1caa]], [[1cad|1cad]], [[1iu5|1iu5]], [[1iu6|1iu6]], [[1qcv|1qcv]], [[1rwd|1rwd]], [[1vcx|1vcx]], [[1zrp|1zrp]], [[4ar3|4ar3]], [[4ar4|4ar4]], [[4ar6|4ar6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bq8|1bq8]], [[1bq9|1bq9]], [[1brf|1brf]], [[1caa|1caa]], [[1cad|1cad]], [[1iu5|1iu5]], [[1iu6|1iu6]], [[1qcv|1qcv]], [[1rwd|1rwd]], [[1vcx|1vcx]], [[1zrp|1zrp]], [[4ar3|4ar3]], [[4ar4|4ar4]], [[4ar6|4ar6]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ar5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar5 OCA], [https://pdbe.org/4ar5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ar5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ar5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RUBR_PYRFU RUBR_PYRFU]] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | ||
<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: Atcc 43587]] | [[Category: Atcc 43587]] | ||
[[Category: Large Structures]] | |||
[[Category: Blakeley, M P]] | [[Category: Blakeley, M P]] | ||
[[Category: Cuypers, M G]] | [[Category: Cuypers, M G]] |
Revision as of 08:43, 25 August 2022
X-ray crystallographic structure of the oxidised form perdeuterated Pyrococcus furiosus rubredoxin in D2O at 295K (in quartz capillary) to 1.00 Angstrom resolution.X-ray crystallographic structure of the oxidised form perdeuterated Pyrococcus furiosus rubredoxin in D2O at 295K (in quartz capillary) to 1.00 Angstrom resolution.
Structural highlights
Function[RUBR_PYRFU] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Publication Abstract from PubMedNeutron crystallographic analyses at near-atomic resolution are presented for both reduced and oxidized forms of perdeuterated Pyrococcus furiosus rubredoxin, a small iron-sulfur redox protein with remarkable thermostability. Hydronium ions may play a key role in the protonation and charge-transfer processes associated with the oxidized and reduced forms of the protein. Picture: overall structure showing D(3) O(+) ions (red and gray molecules). Near-Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes.,Cuypers MG, Mason SA, Blakeley MP, Mitchell EP, Haertlein M, Forsyth VT Angew Chem Int Ed Engl. 2013 Jan 14;52(3):1022-5. doi: 10.1002/anie.201207071., Epub 2012 Dec 6. PMID:23225503[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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