6gwi
From Proteopedia
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<StructureSection load='6gwi' size='340' side='right'caption='[[6gwi]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6gwi' size='340' side='right'caption='[[6gwi]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6gwi]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GWI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gwi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haled Haled]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GWI FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spuC, HELO_1904 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=768066 HALED])</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=6gwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwi OCA], [http://pdbe.org/6gwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gwi RCSB], [http://www.ebi.ac.uk/pdbsum/6gwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwi ProSAT]</span></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=6gwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwi OCA], [http://pdbe.org/6gwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gwi RCSB], [http://www.ebi.ac.uk/pdbsum/6gwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6gwi" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Haled]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gourlay, L J]] | [[Category: Gourlay, L J]] | ||
[[Category: Amino-transferase]] | [[Category: Amino-transferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 17:19, 14 August 2019
The crystal structure of Halomonas elongata amino-transferase
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