View source for 6ez3


==Structure of CDPS from Staphylococcus haemolyticus==
<StructureSection load='6ez3' size='340' side='right'caption='[[6ez3]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ez3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_haemolyticus_JCSC1435 Staphylococcus haemolyticus JCSC1435]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EZ3 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ez3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ez3 OCA], [https://pdbe.org/6ez3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ez3 RCSB], [https://www.ebi.ac.uk/pdbsum/6ez3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ez3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDLS_STAHJ CDLS_STAHJ] It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu) (cLL) from L-leucyl-tRNA(Leu). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine and L-methionine, into cyclodipeptides.<ref>PMID:19430487</ref> 
<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 6ez3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus haemolyticus JCSC1435]]
[[Category: Bourgeois G]]
[[Category: Mechulam Y]]
[[Category: Schmitt E]]