4ar4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ar4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AR4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ar4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AR4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D3O:TRIDEUTERIOOXIDANIUM'>D3O</scene>, <scene name='pdbligand=D8U:DEUTERIUM(1+)'>D8U</scene>, <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">Neutron Diffraction, [[Resolution|Resolution]] 1.381Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D3O:TRIDEUTERIOOXIDANIUM'>D3O</scene>, <scene name='pdbligand=D8U:DEUTERIUM(1+)'>D8U</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4ar4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar4 OCA], [https://pdbe.org/4ar4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ar4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ar4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar4 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=4ar4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ar4 OCA], [https://pdbe.org/4ar4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ar4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ar4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ar4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 09:00, 19 June 2024
Neutron crystallographic structure of the reduced form perdeuterated Pyrococcus furiosus rubredoxin to 1.38 Angstrom resolution.Neutron crystallographic structure of the reduced form perdeuterated Pyrococcus furiosus rubredoxin to 1.38 Angstrom resolution.
Structural highlights
FunctionRUBR_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. See AlsoReferences
|
| ||||||||||||||||||