4azd

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(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...)
Current revision (11:39, 20 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4azd is ON HOLD
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==T57V mutant of aspartate decarboxylase==
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<StructureSection load='4azd' size='340' side='right'caption='[[4azd]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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.R., Abell, C.
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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>
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Description: T57V mutant of aspartate decarboxylase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4azd" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]]
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Abell C]]
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[[Category: Blundell TL]]
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[[Category: Kershaw T]]
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[[Category: Kilkenny ML]]
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[[Category: Lobley CMC]]
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[[Category: Lovelock S]]
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[[Category: Pearson AR]]
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[[Category: Smith AG]]
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[[Category: Webb ME]]
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[[Category: Yorke BA]]

Current revision

T57V mutant of aspartate decarboxylase

PDB ID 4azd

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