View source for 5mlq


==Structure of CDPS from Nocardia brasiliensis==
<StructureSection load='5mlq' size='340' side='right'caption='[[5mlq]], [[Resolution|resolution]] 3.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mlq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nocardia_brasiliensis_ATCC_700358 Nocardia brasiliensis ATCC 700358]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MLQ 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]] 3.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5mlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mlq OCA], [https://pdbe.org/5mlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mlq RCSB], [https://www.ebi.ac.uk/pdbsum/5mlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mlq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K0F6G5_NOCB7 K0F6G5_NOCB7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides that can be further used for the synthesis of diketopiperazines. It was shown that CDPSs fall into two subfamilies, NYH and XYP, characterized by the presence of specific sequence signatures. However, current understanding of CDPSs only comes from studies of enzymes from the NYH subfamily. The present study reveals the crystal structures of three CDPSs from the XYP subfamily. Comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold. This gives a structural basis for the partition of CDPSs into two subfamilies. Despite these differences, the catalytic residues adopt similar positioning regardless of the subfamily suggesting that the XYP and NYH motifs correspond to two structural solutions to facilitate the reactivity of the catalytic serine residue.

Structural basis for partition of the cyclodipeptide synthases into two subfamilies.,Bourgeois G, Seguin J, Babin M, Belin P, Moutiez M, Mechulam Y, Gondry M, Schmitt E J Struct Biol. 2018 Jul;203(1):17-26. doi: 10.1016/j.jsb.2018.03.001. Epub 2018, Mar 2. PMID:29505829<ref>PMID:29505829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mlq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nocardia brasiliensis ATCC 700358]]
[[Category: Babin M]]
[[Category: Belin P]]
[[Category: Bourgeois G]]
[[Category: Gondry M]]
[[Category: Mechulam Y]]
[[Category: Moutiez M]]
[[Category: Schmitt E]]
[[Category: Seguin J]]