8wou: Difference between revisions
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The | ==The crystal structure of aspartate aminotransferases Lpg0070 from Legionella pneumophila== | ||
<StructureSection load='8wou' size='340' side='right'caption='[[8wou]], [[Resolution|resolution]] 2.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wou]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WOU 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]] 2.14Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8wou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wou OCA], [https://pdbe.org/8wou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wou RCSB], [https://www.ebi.ac.uk/pdbsum/8wou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wou ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A130QXX8_LEGPN A0A130QXX8_LEGPN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Legionella pneumophila aspartate aminotransferase (Lpg0070) is a member of the transaminase and belongs to the pyridoxal 5'-phosphate (PLP)-dependent superfamily. It is responsible for the transfer of alpha-amino between aspartate and alpha-ketoglutarate to form glutamate and oxaloacetate. Here, we report the crystal structure of Lpg0070 at the resolution of 2.14 A and 1.7 A, in apo-form and PLP-bound, respectively. Our structural analysis revealed the specific residues involved in the PLP binding and free form against PLP-bound supported conformational changes before substrate recognition. In vitro enzyme activity proves that the absence of the N-terminal arm reduces the enzyme activity of Lpg0070. These data provide further evidence to support the N-terminal arm plays a crucial role in catalytic activity. | |||
Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila.,Gao Y, Yang X, Hua L, Wang M, Ge Q, Wang W, Wang N, Ma J, Ge H Biochem Biophys Res Commun. 2023 Dec 31;689:149230. doi: , 10.1016/j.bbrc.2023.149230. Epub 2023 Nov 10. PMID:37984176<ref>PMID:37984176</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8wou" style="background-color:#fffaf0;"></div> | ||
[[Category: Hua | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila]] | |||
[[Category: Gao YS]] | |||
[[Category: Hua L]] | |||
[[Category: Xie R]] | |||
Latest revision as of 08:08, 6 December 2023
The crystal structure of aspartate aminotransferases Lpg0070 from Legionella pneumophila
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