4ar5: Difference between revisions

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<StructureSection load='4ar5' size='340' side='right'caption='[[4ar5]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
<StructureSection load='4ar5' size='340' side='right'caption='[[4ar5]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ar5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AR5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ar5]] is a 1 chain structure with sequence from [https://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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</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='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='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://pdbe.org/4ar5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ar5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ar5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar5 ProSAT]</span></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=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 ==
[[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.
[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;">
== 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>
==See Also==
 
*[[Rubredoxin 3D structures|Rubredoxin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Rubredoxin PDB structures|Rubredoxin PDB structures]]
</div>
<div class="pdbe-citations 4ar5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43587]]
[[Category: Large Structures]]
[[Category: Blakeley, M P]]
[[Category: Pyrococcus furiosus]]
[[Category: Cuypers, M G]]
[[Category: Blakeley MP]]
[[Category: Forsyth, V T]]
[[Category: Cuypers MG]]
[[Category: Haertlein, M]]
[[Category: Forsyth VT]]
[[Category: Mason, S A]]
[[Category: Haertlein M]]
[[Category: Mitchell, E P]]
[[Category: Mason SA]]
[[Category: Ambient capillary]]
[[Category: Mitchell EP]]
[[Category: Electron transport]]
[[Category: Perdeuterated]]

Latest revision as of 10:16, 1 May 2024

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

4ar5 is a 1 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

4ar5, resolution 1.00Å

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