4pzp: Difference between revisions
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''' | ==Substrate-free structure of D-alanine carrier protein ligase DltA from Bacillus cereus== | ||
<StructureSection load='4pzp' size='340' side='right' caption='[[4pzp]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pzp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZP FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dhv|3dhv]], [[3fcc|3fcc]], [[3fce|3fce]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-alanine--poly(phosphoribitol)_ligase D-alanine--poly(phosphoribitol) ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.13 6.1.1.13] </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=4pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzp RCSB], [http://www.ebi.ac.uk/pdbsum/4pzp PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
D-alanylation of the lipoteichoic acid on Gram-positive cell wall is dependent on dlt gene-encoded proteins DltA, DltB, DltC and DltD. The D-alanyl carrier protein ligase DltA, as a remote homolog of acyl-(coenzyme A) (CoA) synthetase, cycles through two active conformations for the catalysis of adenylation and subsequent thiolation of D-alanine (D-Ala). The crystal structure of DltA in the absence of any substrate was observed to have a noticeably more disordered pocket for ATP which would explain why DltA has relatively low affinity for ATP in the absence of any D-alanyl carrier. We have previously enabled the thiolation of D-alanine in the presence of CoA as the mimic of D-alanyl carrier protein DltC which carries a 4'-phosphopantetheine group on a serine residue. Here we show that the resulting Michaelis constants in the presence of saturating CoA for both ATP and D-alanine were reduced more than 10 fold as compared to the values obtained in the absence of CoA. The presence of CoA also made DltA ~100-fold more selective on D-alanine over L-alanine. The CoA-enhanced substrate recognition further implies that the ATP and D-alanine substrates of the adenylation reaction are incorporated when the DltA enzyme cycles through its thiolation conformation. | |||
Thiolation-enhanced substrate recognition by D-alanyl carrier protein ligase DltA from Bacillus cereus.,Du L, Luo Y F1000Res. 2014 May 13;3:106. doi: 10.12688/f1000research.4097.1. eCollection, 2014. PMID:25285205<ref>PMID:25285205</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atila, M]] | |||
[[Category: Du, L]] | |||
[[Category: Luo, Y]] | |||
[[Category: Homologous to acetyl-coa synthetase]] | |||
[[Category: Ligase]] | |||
Revision as of 07:49, 26 November 2014
Substrate-free structure of D-alanine carrier protein ligase DltA from Bacillus cereus
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