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7tqr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of histidine ammonia lyase from Thermoplasma acidophilum== | |
| + | <StructureSection load='7tqr' size='340' side='right'caption='[[7tqr]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7tqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TQR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</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=7tqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tqr OCA], [https://pdbe.org/7tqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tqr RCSB], [https://www.ebi.ac.uk/pdbsum/7tqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tqr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HUTH_THEAC HUTH_THEAC] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Extremophile enzymes are useful in biotechnology and biomedicine due to their abilities to withstand harsh environments. The abilities of histidine ammonia lyases from different extremophiles to preserve their catalytic activities after exposure to acid were assessed. Thermoplasma acidophilum histidine ammonia lyase was identified as an enzyme with a promising catalytic profile following acid treatment. The fusion of this enzyme with the maltose-binding protein or co-incubation with the chaperone HdeA further helped Thermoplasma acidophilum histidine ammonia lyase to withstand acid treatments down to pH 2.8. The assembly of a microreactor by encapsulation of MBP-Thermoplasma acidophilum histidine ammonia lyase into a photocrosslinked poly(vinyl alcohol) hydrogel allowed the enzyme to recover over 50% of its enzymatic activity following exposure to simulated gastric and intestinal fluids. Our results show that using engineered proteins obtained from extremophiles in combination with polymer-based encapsulation can advance the oral formulations of biologicals. | ||
| - | + | Microreactor equipped with naturally acid-resistant histidine ammonia lyase from an extremophile.,Ade C, Marcelino TF, Dulchavsky M, Wu K, Bardwell JCA, Stadler B Mater Adv. 2022 Apr 21;3(8):3649-3662. doi: 10.1039/d2ma00051b. Epub 2022 Mar 29. PMID:36238657<ref>PMID:36238657</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7tqr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermoplasma acidophilum]] | ||
| + | [[Category: Bardwell JCA]] | ||
| + | [[Category: Dulchavsky M]] | ||
| + | [[Category: Wu K]] | ||
Current revision
Crystal Structure of histidine ammonia lyase from Thermoplasma acidophilum
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