3mps: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='3mps' size='340' side='right'caption='[[3mps]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mps]] is a 8 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=3MPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MPS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mps]] is a 8 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=3MPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MPS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</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]] 2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pwf|3pwf]], [[3pza|3pza]], [[3qvd|3qvd]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</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=3mps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mps OCA], [http://pdbe.org/3mps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mps RCSB], [http://www.ebi.ac.uk/pdbsum/3mps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mps 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=3mps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mps OCA], [https://pdbe.org/3mps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mps RCSB], [https://www.ebi.ac.uk/pdbsum/3mps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mps ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q9UWP7_9EURY Q9UWP7_9EURY]
-High-resolution crystal structures of Pyrococcus furiosus rubrerythrin (PfRbr) in the resting (all-ferrous) state and at time points following exposure of the crystals to hydrogen peroxide are reported. This approach was possible because of the relativity slow turnover of PfRbr at room temperature. To this end, we were able to perform time-dependent peroxide treatment of the fully reduced enzyme, under strictly anaerobic conditions, in the crystalline state. In this work we demonstrate, for the first time, that turnover of a thermophilic rubrerythrin results in approximately 2-A movement of one iron atom in the diiron site from a histidine to a carboxylate ligand. These results confirm that, despite the domain-swapped architecture, the hyperthermophilic rubrerythrins also utilize the classic combination of iron sites together with redox-dependent iron toggling to selectively reduce hydrogen peroxide over dioxygen. In addition, we have identified previously unobserved intermediates in the reaction cycle and observed structural changes that may explain the enzyme precipitation observed for the all-iron form of PfRbr upon oxidation to the all-ferric state.
-A cryo-crystallographic time course for peroxide reduction by rubrerythrin from Pyrococcus furiosus.,Dillard BD, Demick JM, Adams MW, Lanzilotta WN J Biol Inorg Chem. 2011 Jun 7. PMID:21647777<ref>PMID:21647777</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3mps" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Journal:JBIC:11|Journal:JBIC:11]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
 [[Category: Pyrococcus furiosus]]
-[[Category: Adams, M W.W]]
+[[Category: Adams MWW]]
-[[Category: Dillard, B D]]
+[[Category: Dillard BD]]
-[[Category: Lanzilotta, W N]]
+[[Category: Lanzilotta WN]]
-[[Category: Diiron]]
-[[Category: Oxidized]]
-[[Category: Oxidoreductase]]
-[[Category: Peroxidase]]
-[[Category: Peroxide]]
-[[Category: Rubrerythrin]]