5ocd
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==structure of a CDPS from Fluoribacter dumoffii== | |
| + | <StructureSection load='5ocd' size='340' side='right' caption='[[5ocd]], [[Resolution|resolution]] 3.06Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ocd]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OCD FirstGlance]. <br> | ||
| + | </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=5ocd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ocd OCA], [http://pdbe.org/5ocd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ocd RCSB], [http://www.ebi.ac.uk/pdbsum/5ocd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ocd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ocd" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bourgeois, G]] | [[Category: Bourgeois, G]] | ||
[[Category: Mechulam, Y]] | [[Category: Mechulam, Y]] | ||
| + | [[Category: Schmitt, E]] | ||
| + | [[Category: Cdp]] | ||
| + | [[Category: Non ribosomal peptide synthesis]] | ||
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Trna]] | ||
Revision as of 18:34, 1 August 2018
structure of a CDPS from Fluoribacter dumoffii
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