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==Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.==
==Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.==
<StructureSection load='6f2h' size='340' side='right' caption='[[6f2h]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
<StructureSection load='6f2h' size='340' side='right'caption='[[6f2h]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6f2h]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2H FirstGlance]. <br>
<table><tr><td colspan='2'>[[6f2h]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F2H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7MT:1,4-Bis((6-carboxypyridin-2-yl)methyl)-1,4,7-triazacyclononane'>7MT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</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]] 2.19&#8491;</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=6f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2h OCA], [http://pdbe.org/6f2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2h RCSB], [http://www.ebi.ac.uk/pdbsum/6f2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2h ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7MT:Tb-Xo4'>7MT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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'>[https://proteopedia.org/fgij/fg.htm?mol=6f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2h OCA], [https://pdbe.org/6f2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f2h RCSB], [https://www.ebi.ac.uk/pdbsum/6f2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[https://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dumont, E]]
[[Category: Large Structures]]
[[Category: Engilberge, S]]
[[Category: Pyrococcus horikoshii]]
[[Category: Franzetti, B]]
[[Category: Di Pietro S]]
[[Category: Girard, E]]
[[Category: Dumont E]]
[[Category: Maury, O]]
[[Category: Engilberge S]]
[[Category: Pietro, S Di]]
[[Category: Franzetti B]]
[[Category: Riobe, F]]
[[Category: Girard E]]
[[Category: Crystallophore]]
[[Category: Maury O]]
[[Category: Hydrolase]]
[[Category: Riobe F]]
[[Category: Nucleation]]
[[Category: Phasing]]
[[Category: Protease]]
[[Category: Tb-xo4]]

Latest revision as of 12:24, 9 May 2024

Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.

6f2h, resolution 2.19Å

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