6gwi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of Halomonas elongata amino-transferase== |
| + | <StructureSection load='6gwi' size='340' side='right'caption='[[6gwi]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </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]] | ||
Current revision
The crystal structure of Halomonas elongata amino-transferase
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