View source for 5vk7


==aspartate aminotransferase pH 4.0==
<StructureSection load='5vk7' size='340' side='right'caption='[[5vk7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vk7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VK7 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=5vk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vk7 OCA], [https://pdbe.org/5vk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vk7 RCSB], [https://www.ebi.ac.uk/pdbsum/5vk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vk7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AATC_PIG AATC_PIG] Plays a key role in amino acid metabolism.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes dependent on pyridoxal 5'-phosphate (PLP, the active form of vitamin B6) perform a myriad of diverse chemical transformations. They promote various reactions by modulating the electronic states of PLP through weak interactions in the active site. Neutron crystallography has the unique ability of visualizing the nuclear positions of hydrogen atoms in macromolecules. Here we present a room-temperature neutron structure of a homodimeric PLP-dependent enzyme, aspartate aminotransferase, which was reacted in situ with alpha-methylaspartate. In one monomer, the PLP remained as an internal aldimine with a deprotonated Schiff base. In the second monomer, the external aldimine formed with the substrate analog. We observe a deuterium equidistant between the Schiff base and the C-terminal carboxylate of the substrate, a position indicative of a low-barrier hydrogen bond. Quantum chemical calculations and a low-pH room-temperature X-ray structure provide insight into the physical phenomena that control the electronic modulation in aspartate aminotransferase.Pyridoxal 5'-phosphate (PLP) is a ubiquitous co factor for diverse enzymes, among them aspartate aminotransferase. Here the authors use neutron crystallography, which allows the visualization of the positions of hydrogen atoms, and computation to characterize the catalytic mechanism of the enzyme.

Direct visualization of critical hydrogen atoms in a pyridoxal 5'-phosphate enzyme.,Dajnowicz S, Johnston RC, Parks JM, Blakeley MP, Keen DA, Weiss KL, Gerlits O, Kovalevsky A, Mueser TC Nat Commun. 2017 Oct 16;8(1):955. doi: 10.1038/s41467-017-01060-y. PMID:29038582<ref>PMID:29038582</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vk7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Dajnowicz S]]
[[Category: Kovalevsky AY]]
[[Category: Mueser TC]]