5k3w: Difference between revisions
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==Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum== | |||
<StructureSection load='5k3w' size='340' side='right'caption='[[5k3w]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5k3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Curtobacterium_pusillum Curtobacterium pusillum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K3W 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]] 2.503Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAB:3-AMINOBENZOIC+ACID'>GAB</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=5k3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k3w OCA], [https://pdbe.org/5k3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k3w RCSB], [https://www.ebi.ac.uk/pdbsum/5k3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k3w ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1S4NYF0_9MICO A0A1S4NYF0_9MICO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 A. It shows significant differences especially in the active site compared to other transaminases of the fold IV family and thus indicates the existence of a new subgroup within this family. Although the discovered transaminases were not able to convert ketones in a reasonable time frame, overall, the enrichment-based approach was successful, as we identified two amine transaminases, which convert (R)-amines with high enantioselectivity, and can be used for a kinetic resolution of 1-phenylethylamine and analogues to obtain the (S)-amines with e.e.s >99%. | |||
Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.,Pavkov-Keller T, Strohmeier GA, Diepold M, Peeters W, Smeets N, Schurmann M, Gruber K, Schwab H, Steiner K Sci Rep. 2016 Dec 1;6:38183. doi: 10.1038/srep38183. PMID:27905516<ref>PMID:27905516</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5k3w" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Curtobacterium pusillum]] | |||
[[Category: Large Structures]] | |||
[[Category: Diepold M]] | |||
[[Category: Gruber K]] | |||
[[Category: Pavkov-Keller T]] | |||
[[Category: Steiner K]] | |||
Latest revision as of 13:39, 27 September 2023
Structural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillumStructural characterisation of fold IV-transaminase, CpuTA1, from Curtobacterium pusillum
Structural highlights
FunctionPublication Abstract from PubMedTransaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 A. It shows significant differences especially in the active site compared to other transaminases of the fold IV family and thus indicates the existence of a new subgroup within this family. Although the discovered transaminases were not able to convert ketones in a reasonable time frame, overall, the enrichment-based approach was successful, as we identified two amine transaminases, which convert (R)-amines with high enantioselectivity, and can be used for a kinetic resolution of 1-phenylethylamine and analogues to obtain the (S)-amines with e.e.s >99%. Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.,Pavkov-Keller T, Strohmeier GA, Diepold M, Peeters W, Smeets N, Schurmann M, Gruber K, Schwab H, Steiner K Sci Rep. 2016 Dec 1;6:38183. doi: 10.1038/srep38183. PMID:27905516[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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