View source for 8onj


==Crystal structure of D-amino acid aminotransferase from Aminobacterium colombiense point mutant R88L==
<StructureSection load='8onj' size='340' side='right'caption='[[8onj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8onj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aminobacterium_colombiense Aminobacterium colombiense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ONJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ONJ 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8onj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8onj OCA], [https://pdbe.org/8onj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8onj RCSB], [https://www.ebi.ac.uk/pdbsum/8onj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8onj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5EHC5_AMICL D5EHC5_AMICL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The development of biocatalysts requires reorganization of the enzyme's active site to facilitate the productive binding of the target substrate and improve turnover number at desired conditions. Pyridoxal-5'-phosphate (PLP) - dependent transaminases are highly efficient biocatalysts for asymmetric amination of ketones and keto acids. However, transaminases, being stereoselective enzymes, have a narrow substrate specificity due to the ordered structure of the active site and work only in neutral-alkaline media. Here, we investigated the d-amino acid transaminase from Aminobacterium colombiense, with the active site organized differently from that of the canonical d-amino acid transaminase from Bacillus sp. YM-1. Using a combination of site-directed mutagenesis, kinetic analysis, molecular modeling, and structural analysis we determined the active site residues responsible for substrate binding, substrate differentiation, thermostability of a functional dimer, and affecting the pH optimum. We demonstrated that the high specificity toward d-glutamate/alpha-ketoglutarate is due to the interactions of a gamma-carboxylate group with K237 residue, while binding of other substrates stems from the effectiveness of their accommodation in the active site optimized for d-glutamate/alpha-ketoglutarate binding. Furthermore, we showed that the K237A substitution shifts the catalytic activity optimum to acidic pH. Our findings are useful for achieving target substrate specificity and demonstrate the potential for developing and optimizing transaminases for various applications.

In search for structural targets for engineering d-amino acid transaminase: modulation of pH optimum and substrate specificity.,Shilova SA, Matyuta IO, Khrenova MG, Nikolaeva AY, Klyachko NL, Minyaev ME, Khomutov AR, Boyko KM, Popov VO, Bezsudnova EY Biochem J. 2023 Aug 30;480(16):1267-1284. doi: 10.1042/BCJ20230233. PMID:37548495<ref>PMID:37548495</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8onj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aminobacterium colombiense]]
[[Category: Large Structures]]
[[Category: Bezsudnova EY]]
[[Category: Boyko KM]]
[[Category: Matyuta IO]]
[[Category: Minyaev ME]]
[[Category: Popov VO]]
[[Category: Shilova SA]]