View source for 6zup


==Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6 cocrystalized with substrate analog - L-(-)-3-phenyllactic acid==
<StructureSection load='6zup' size='340' side='right'caption='[[6zup]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6zup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Psychrobacter_sp._B6 Psychrobacter sp. B6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZUP 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HFA:ALPHA-HYDROXY-BETA-PHENYL-PROPIONIC+ACID'>HFA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=6zup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zup OCA], [https://pdbe.org/6zup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zup RCSB], [https://www.ebi.ac.uk/pdbsum/6zup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zup ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C7E5X4_9GAMM C7E5X4_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aromatic amino acid aminotransferases present a special potential in the production of drugs and synthons, thanks to their ability to accommodate a wider range of substrates in their active site, in contrast to aliphatic amino acid aminotransferases. The mechanism of active site adjustment toward substrates of psychrophilic aromatic amino acid aminotransferase (PsyArAT) from Psychrobacter sp. B6 is discussed based on crystal structures of complexes with four hydroxy-analogs of substrates: phenylalanine, tyrosine, tryptophan and aspartic acid. These competitive inhibitors are bound in the active center of PsyArAT but do not undergo transamination reaction, which makes them an outstanding tool for examination of the enzyme catalytic center. The use of hydroxy-acids enabled insight into substrate binding by native PsyArAT, without mutating the catalytic lysine and modifying cofactor interactions. Thus, the binding mode of substrates and the resulting analysis of the volume of the catalytic site is close to a native condition. Observation of these inhibitors' binding allows for explanation of the enzyme's adaptability to process various sizes of substrates and to gain knowledge about its potential biotechnological application. Depending on the character and size of the used inhibitors, the enzyme crystallized in different space groups and showed conformational changes of the active site upon ligand binding.

Structural Evidence of Active Site Adaptability towards Different Sized Substrates of Aromatic Amino Acid Aminotransferase from Psychrobacter Sp. B6.,Bujacz A, Rum J, Rutkiewicz M, Pietrzyk-Brzezinska AJ, Bujacz G Materials (Basel). 2021 Jun 17;14(12). pii: ma14123351. doi: 10.3390/ma14123351. PMID:34204354<ref>PMID:34204354</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6zup" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Psychrobacter sp. B6]]
[[Category: Bujacz A]]
[[Category: Bujacz G]]
[[Category: Pietrzyk-Brzezinska AJ]]
[[Category: Rum J]]
[[Category: Rutkiewicz M]]