4azd: Difference between revisions
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==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 [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AZD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aw8|1aw8]], [[1ppy|1ppy]], [[1pqe|1pqe]], [[1pqf|1pqf]], [[1pqh|1pqh]], [[1pt0|1pt0]], [[1pt1|1pt1]], [[1pyq|1pyq]], [[1pyu|1pyu]], [[4aok|4aok]], [[4aon|4aon]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4azd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4azd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4azd RCSB], [http://www.ebi.ac.uk/pdbsum/4azd PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> | |||
== | ==See Also== | ||
*[[Aspartate decarboxylase|Aspartate decarboxylase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspartate 1-decarboxylase]] | [[Category: Aspartate 1-decarboxylase]] | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Abell, C | [[Category: Abell, C]] | ||
[[Category: Blundell, T L | [[Category: Blundell, T L]] | ||
[[Category: Kershaw, T | [[Category: Kershaw, T]] | ||
[[Category: Kilkenny, M L | [[Category: Kilkenny, M L]] | ||
[[Category: Lobley, C M.C | [[Category: Lobley, C M.C]] | ||
[[Category: Lovelock, S | [[Category: Lovelock, S]] | ||
[[Category: Pearson, A R | [[Category: Pearson, A R]] | ||
[[Category: Smith, A G | [[Category: Smith, A G]] | ||
[[Category: Webb, M E | [[Category: Webb, M E]] | ||
[[Category: Yorke, B A | [[Category: Yorke, B A]] | ||
[[Category: Amino acid substitution]] | [[Category: Amino acid substitution]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 08:17, 25 December 2014
T57V mutant of aspartate decarboxylase
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