View source for 7azu


==Crystal structure of a cyclodipeptide synthase from Bacillus thermoamylovorans==
<StructureSection load='7azu' size='340' side='right'caption='[[7azu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7azu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldibacillus_thermoamylovorans Caldibacillus thermoamylovorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AZU 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]] 1.801&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0RE:(2S)-HEXANE-1,2-DIOL'>0RE</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=7azu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7azu OCA], [https://pdbe.org/7azu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7azu RCSB], [https://www.ebi.ac.uk/pdbsum/7azu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7azu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A090KS30_9BACI A0A090KS30_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclodipeptide synthases (CDPSs) produce a variety of cyclic dipeptide products by utilising two aminoacylated tRNA substrates. We sought to investigate the minimal requirements for substrate usage in this class of enzymes as the relationship between CDPSs and their substrates remains elusive. Here, we investigated the Bacillus thermoamylovorans enzyme, BtCDPS, which synthesises cyclo(l-Leu-l-Leu). We systematically tested where specificity arises and, in the process, uncovered small molecules (activated amino esters) that will suffice as substrates, although catalytically poor. We solved the structure of BtCDPS to 1.7 A and combining crystallography, enzymatic assays and substrate docking experiments propose a model for how the minimal substrates interact with the enzyme. This work is the first report of a CDPS enzyme utilizing a molecule other than aa-tRNA as a substrate; providing insights into substrate requirements and setting the stage for the design of improved simpler substrates.

Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme.,Harding CJ, Sutherland E, Hanna JG, Houston DR, Czekster CM RSC Chem Biol. 2021 Jan 15;2(1):230-240. doi: 10.1039/d0cb00142b. PMID:33937777<ref>PMID:33937777</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7azu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caldibacillus thermoamylovorans]]
[[Category: Large Structures]]
[[Category: Czekster CM]]
[[Category: Harding CJ]]