View source for 6gwi


==The crystal structure of Halomonas elongata amino-transferase==
<StructureSection load='6gwi' size='340' side='right'caption='[[6gwi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gwi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Halomonas_elongata_DSM_2581 Halomonas elongata DSM 2581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GWI 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6gwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwi OCA], [https://pdbe.org/6gwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gwi RCSB], [https://www.ebi.ac.uk/pdbsum/6gwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E1V913_HALED E1V913_HALED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Directed evolution of transaminases is a widespread technique in the development of highly sought-after biocatalysts for industrial applications. This process, however, is challenged by the limited availability of effective high-throughput protocols to evaluate mutant libraries. Here we report a rapid, reliable, and widely applicable background depletion method for solid-phase screening of transaminase variants, which was successfully applied to a transaminase from Halomonas elongata (HEWT), evolved through rounds of random mutagenesis towards a series of diverse prochiral ketones. This approach enabled the identification of transaminase variants in viable cells with significantly improved activity towards para-substituted acetophenones (up to 60-fold), as well as tetrahydrothiophen-3-one and related substrates. Rationalisation of the mutants was assisted by determination of the high-resolution wild-type HEWT crystal structure presented herein.

Widely applicable background depletion step enables transaminase evolution through solid-phase screening.,Planchestainer M, Hegarty E, Heckmann CM, Gourlay LJ, Paradisi F Chem Sci. 2019 May 9;10(23):5952-5958. doi: 10.1039/c8sc05712e. eCollection 2019 , Jun 21. PMID:31360401<ref>PMID:31360401</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gwi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Halomonas elongata DSM 2581]]
[[Category: Large Structures]]
[[Category: Gourlay LJ]]