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==Crystal structure of Pseudomonas stutzeri D-phenylglycine aminotransferase==
==Crystal structure of Pseudomonas stutzeri D-phenylglycine aminotransferase==
<StructureSection load='6dvs' size='340' side='right' caption='[[6dvs]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='6dvs' size='340' side='right'caption='[[6dvs]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6dvs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_sewerinii"_bergey_et_al._1923 "achromobacter sewerinii" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DVS FirstGlance]. <br>
<table><tr><td colspan='2'>[[6dvs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DVS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.821&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dpgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-4-hydroxyphenylglycine_transaminase D-4-hydroxyphenylglycine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.72 2.6.1.72] </span></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=6dvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dvs OCA], [https://pdbe.org/6dvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dvs RCSB], [https://www.ebi.ac.uk/pdbsum/6dvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dvs 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=6dvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dvs OCA], [http://pdbe.org/6dvs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dvs RCSB], [http://www.ebi.ac.uk/pdbsum/6dvs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dvs ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q6VY99_STUST Q6VY99_STUST]
Aromatic d-amino acids are key precursors for the production of many small molecule therapeutics. Therefore, the development of biocatalytic methods for their synthesis is of great interest. An enzyme that has great potential as a biocatalyst for the synthesis of d-amino acids is the stereoinverting d-phenylglycine aminotransferase (DPAT) from Pseudomonas stutzeri ST-201. This enzyme catalyzes a unique l to d transamination reaction that produces d-phenylglycine and alpha-ketoglutarate from benzoylformate and l-glutamate, via a mechanism that is poorly understood. Here, we present the crystal structure of DPAT, which shows that the enzyme folds into a two-domain structure representative of class III aminotransferases. Guided by the crystal structure, we performed saturation mutagenesis to probe the substrate binding pockets of the enzyme. These experiments helped us identify two arginine residues (R34 and R407), one in each binding pocket, that are essential to catalysis. Together with kinetic analyses using a library of amino acid substrates, our mutagenesis and structural studies allow us to propose a binding model that explains the dual l/d specificity of DPAT. Our kinetic analyses also demonstrate that DPAT can catalyze the transamination of beta- and gamma-amino acids, reclassifying this enzyme as an omega-aminotransferase. Collectively, our studies highlight that the DPAT active site is amenable to protein engineering for expansion of its substrate scope, which offers the opportunity to generate new biocatalysts for the synthesis of a variety of valuable optically pure d-amino acids from inexpensive and abundant l-amino acids.


Structural Determinants of the Stereoinverting Activity of Pseudomonas stutzeri d-Phenylglycine Aminotransferase.,Walton CJW, Thiebaut F, Brunzelle JS, Couture JF, Chica RA Biochemistry. 2018 Sep 7. doi: 10.1021/acs.biochem.8b00767. PMID:30153007<ref>PMID:30153007</ref>
==See Also==
 
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6dvs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Achromobacter sewerinii bergey et al. 1923]]
[[Category: Large Structures]]
[[Category: D-4-hydroxyphenylglycine transaminase]]
[[Category: Pseudomonas stutzeri]]
[[Category: Chica, R]]
[[Category: Chica R]]
[[Category: Couture, J F]]
[[Category: Couture JF]]
[[Category: Aminotransferase]]
[[Category: Transferase]]

Latest revision as of 17:37, 13 March 2024

Crystal structure of Pseudomonas stutzeri D-phenylglycine aminotransferaseCrystal structure of Pseudomonas stutzeri D-phenylglycine aminotransferase

Structural highlights

6dvs is a 1 chain structure with sequence from Pseudomonas stutzeri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.821Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6VY99_STUST

See Also

6dvs, resolution 1.82Å

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