View source for 4pzp


==Substrate-free structure of D-alanine carrier protein ligase DltA from Bacillus cereus==
<StructureSection load='4pzp' size='340' side='right'caption='[[4pzp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pzp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4PZP 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]] 1.9&#8491;</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=4pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzp OCA], [https://pdbe.org/4pzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzp RCSB], [https://www.ebi.ac.uk/pdbsum/4pzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DLTA_BACCR DLTA_BACCR] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp (By similarity).
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pzp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus cereus ATCC 14579]]
[[Category: Large Structures]]
[[Category: Atila M]]
[[Category: Du L]]
[[Category: Luo Y]]