View source for 8huy


==N-acetyl-(R)-beta-phenylalanine acylase==
<StructureSection load='8huy' size='340' side='right'caption='[[8huy]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8huy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia Burkholderia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HUY 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]] 2.45&#8491;</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=8huy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8huy OCA], [https://pdbe.org/8huy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8huy RCSB], [https://www.ebi.ac.uk/pdbsum/8huy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8huy ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-Acetyl-(R)-beta-phenylalanine acylase is an enzyme that hydrolyzes the amide bond of N-acetyl-(R)-beta-phenylalanine to produce enantiopure (R)-beta-phenylalanine. In previous studies, Burkholderia sp. AJ110349 and Variovorax sp. AJ110348 were isolated as (R)-enantiomer-specific N-acetyl-(R)-beta-phenylalanine acylase-producing organisms and the properties of the native enzyme from Burkholderia sp. AJ110349 were characterized. In this study, structural analyses were carried out in order to investigate the structure-function relationships of the enzymes derived from both organisms. The recombinant N-acetyl-(R)-beta-phenylalanine acylases were crystallized by the hanging-drop vapor-diffusion method under multiple crystallization solution conditions. The crystals of the Burkholderia enzyme belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 112.70-112.97, c = 341.50-343.32 A, and were likely to contain two subunits in the asymmetric unit. The crystal structure was solved by the Se-SAD method, suggesting that two subunits in the asymmetric unit form a dimer. Each subunit was composed of three domains, and they showed structural similarity to the corresponding domains of the large subunit of N,N-dimethylformamidase from Paracoccus sp. strain DMF. The crystals of the Variovorax enzyme grew as twinned crystals and were not suitable for structure determination. Using size-exclusion chromatography with online static light-scattering analysis, the N-acetyl-(R)-beta-phenylalanine acylases were clarified to be dimeric in solution.

Expression, purification and crystallization of N-acetyl-(R)-beta-phenylalanine acylases derived from Burkholderia sp. AJ110349 and Variovorax sp. AJ110348 and structure determination of the Burkholderia enzyme.,Kato Y, Kawasaki H, Nakamatsu T, Matsuda N, Natsume R Acta Crystallogr F Struct Biol Commun. 2023 Mar 1;79(Pt 3):70-78. doi: , 10.1107/S2053230X23000730. Epub 2023 Feb 23. PMID:36862095<ref>PMID:36862095</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8huy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Burkholderia]]
[[Category: Large Structures]]
[[Category: Kato Y]]
[[Category: Natsume R]]