4ar5
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==X-ray crystallographic structure of the oxidised form perdeuterated Pyrococcus furiosus rubredoxin in D2O at 295K (in quartz capillary) to 1.00 Angstom resolution.== |
| + | <StructureSection load='4ar5' size='340' side='right' caption='[[4ar5]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ar5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. 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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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='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=4ar5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ar5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ar5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Neutron 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<ref>PMID:23225503</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
| - | [[Category: Blakeley, M P | + | [[Category: Blakeley, M P]] |
| - | [[Category: Cuypers, M G | + | [[Category: Cuypers, M G]] |
| - | [[Category: Forsyth, V T | + | [[Category: Forsyth, V T]] |
| - | [[Category: Haertlein, M | + | [[Category: Haertlein, M]] |
| - | [[Category: Mason, S A | + | [[Category: Mason, S A]] |
| - | [[Category: Mitchell, E P | + | [[Category: Mitchell, E P]] |
[[Category: Ambient capillary]] | [[Category: Ambient capillary]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Perdeuterated]] | [[Category: Perdeuterated]] | ||
Revision as of 03:14, 25 December 2014
X-ray crystallographic structure of the oxidised form perdeuterated Pyrococcus furiosus rubredoxin in D2O at 295K (in quartz capillary) to 1.00 Angstom resolution.
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