View source for 6xwb


==Crystal structure of an R-selective transaminase from Thermomyces stellatus.==
<StructureSection load='6xwb' size='340' side='right'caption='[[6xwb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xwb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_stellatus Thermomyces stellatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWB 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6xwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwb OCA], [https://pdbe.org/6xwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwb RCSB], [https://www.ebi.ac.uk/pdbsum/6xwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwb ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The identification and 3D structural characterization of a homolog of the (R)-selective transaminase (RTA) from Aspergillus terreus (AtRTA), from the thermotolerant fungus Thermomyces stellatus (TsRTA) is here reported. The thermostability of TsRTA (40% retained activity after 7 days at 40 degrees C) was initially attributed to its tetrameric form in solution, however subsequent studies of AtRTA revealed it also exists predominantly as a tetramer yet, at 40 degrees C, it is inactivated within 48 h. The engineering of a cysteine residue to promote disulfide bond formation across the dimer-dimer interface stabilized both enzymes, with TsRTA_G205C retaining almost full activity after incubation at 50 degrees C for 7 days. Thus, the role of this mutation was elucidated and the importance of stabilizing the tetramer for overall stability of RTAs is highlighted. TsRTA accepts the common amine donors (R)-methylbenzylamine, isopropylamine, and d-alanine as well as aromatic and aliphatic ketones and aldehydes.

An (R)-Selective Transaminase From Thermomyces stellatus: Stabilizing the Tetrameric Form.,Heckmann CM, Gourlay LJ, Dominguez B, Paradisi F Front Bioeng Biotechnol. 2020 Jul 22;8:707. doi: 10.3389/fbioe.2020.00707., eCollection 2020. PMID:32793563<ref>PMID:32793563</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xwb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomyces stellatus]]
[[Category: Gourlay LJ]]