4azd: Difference between revisions
New page: '''Unreleased structure''' The entry 4azd is ON HOLD Authors: Webb, M.E., Yorke, B.A., Kershaw, T., Lovelock, S., Lobley, C.M.C., Kilkenny, M.L., Smith, A.G., Blundell, T.L., Pearson, A... |
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The | ==T57V mutant of aspartate decarboxylase== | ||
<StructureSection load='4azd' size='340' side='right'caption='[[4azd]], [[Resolution|resolution]] 1.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4azd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AZD 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]] 1.62Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=4azd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azd OCA], [https://pdbe.org/4azd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4azd RCSB], [https://www.ebi.ac.uk/pdbsum/4azd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4azd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aspartate alpha-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of beta-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formed via the intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation. | |||
Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase.,Webb ME, Yorke BA, Kershaw T, Lovelock S, Lobley CM, Kilkenny ML, Smith AG, Blundell TL, Pearson AR, Abell C Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1166-72. doi:, 10.1107/S1399004713034275. Epub 2014 Mar 21. PMID:24699660<ref>PMID:24699660</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4azd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]] | |||
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Abell C]] | |||
[[Category: Blundell TL]] | |||
[[Category: Kershaw T]] | |||
[[Category: Kilkenny ML]] | |||
[[Category: Lobley CMC]] | |||
[[Category: Lovelock S]] | |||
[[Category: Pearson AR]] | |||
[[Category: Smith AG]] | |||
[[Category: Webb ME]] | |||
[[Category: Yorke BA]] | |||