6f2f: Difference between revisions
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==Crystal structure of Protease 1 from Pyrococcus Horikoshii co-cystallized in presence of 10 mM Tb-Xo4 and ammonium sulfate.== | |||
<StructureSection load='6f2f' size='340' side='right' caption='[[6f2f]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f2f]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2F FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2HA:DIHYDROXYACETONE'>2HA</scene>, <scene name='pdbligand=7MT:1,4-Bis((6-carboxypyridin-2-yl)methyl)-1,4,7-triazacyclononane'>7MT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</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=6f2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2f OCA], [http://pdbe.org/6f2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2f RCSB], [http://www.ebi.ac.uk/pdbsum/6f2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DEGLY_PYRHO DEGLY_PYRHO]] Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Also displays proteolytic activity (PubMed:11114201).[UniProtKB:Q51732]<ref>PMID:11114201</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystallophores are lanthanide complexes that act as powerful auxiliary for protein crystallography due to their strong nucleating and phasing effects. To get first insights on the mechanisms behind nucleation induced by Crystallophore, we systematically identified various elaborated networks of supramolecular interactions between Tb-Xo4 and subset of 6 protein structures determined by X-ray diffraction in complex with terbium-Crystallophore (Tb-Xo4). Such interaction mapping analyses demonstrate the versatile binding behavior of the Crystallophore and pave the way to a better understanding of its unique properties. | |||
Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography.,Engilberge S, Riobe F, Wagner T, Di Pietro S, Breyton C, Franzetti B, Shima S, Girard E, Dumont E, Maury O Chemistry. 2018 Jul 11;24(39):9739-9746. doi: 10.1002/chem.201802172. Epub 2018, Jun 25. PMID:29806881<ref>PMID:29806881</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6f2f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dumont, E]] | [[Category: Dumont, E]] | ||
[[Category: Engilberge, S]] | |||
[[Category: Franzetti, B]] | [[Category: Franzetti, B]] | ||
[[Category: | [[Category: Girard, E]] | ||
[[Category: Maury, O]] | |||
[[Category: Pietro, S Di]] | |||
[[Category: Riobe, F]] | [[Category: Riobe, F]] | ||
[[Category: | [[Category: Cell cycle]] | ||
[[Category: Crystallophore]] | |||
[[Category: Lanthanide complex]] | |||
[[Category: Nucleation]] | |||
[[Category: Phasing]] | |||
[[Category: Tb-xo4]] | |||
Revision as of 10:50, 3 October 2018
Crystal structure of Protease 1 from Pyrococcus Horikoshii co-cystallized in presence of 10 mM Tb-Xo4 and ammonium sulfate.Crystal structure of Protease 1 from Pyrococcus Horikoshii co-cystallized in presence of 10 mM Tb-Xo4 and ammonium sulfate.
Structural highlights
Function[DEGLY_PYRHO] Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Also displays proteolytic activity (PubMed:11114201).[UniProtKB:Q51732][1] Publication Abstract from PubMedCrystallophores are lanthanide complexes that act as powerful auxiliary for protein crystallography due to their strong nucleating and phasing effects. To get first insights on the mechanisms behind nucleation induced by Crystallophore, we systematically identified various elaborated networks of supramolecular interactions between Tb-Xo4 and subset of 6 protein structures determined by X-ray diffraction in complex with terbium-Crystallophore (Tb-Xo4). Such interaction mapping analyses demonstrate the versatile binding behavior of the Crystallophore and pave the way to a better understanding of its unique properties. Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography.,Engilberge S, Riobe F, Wagner T, Di Pietro S, Breyton C, Franzetti B, Shima S, Girard E, Dumont E, Maury O Chemistry. 2018 Jul 11;24(39):9739-9746. doi: 10.1002/chem.201802172. Epub 2018, Jun 25. PMID:29806881[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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