View source for 5isx


==Structure of the holo PCP-E didomain of the gramicidin S synthetase A==
<StructureSection load='5isx' size='340' side='right'caption='[[5isx]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5isx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ISX 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]] 2.335&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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=5isx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isx OCA], [https://pdbe.org/5isx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5isx RCSB], [https://www.ebi.ac.uk/pdbsum/5isx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5isx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRSA_BREBE GRSA_BREBE] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nonribosomal peptide synthetases are large, complex multidomain enzymes responsible for the biosynthesis of a wide range of peptidic natural products. Inherent to synthetase chemistry is the thioester templated mechanism that relies on protein/protein interactions and interdomain dynamics. Several questions related to structure and mechanism remain to be addressed, including the incorporation of accessory domains and intermodule interactions. The inclusion of nonproteinogenic d-amino acids into peptide frameworks is a common and important modification for bioactive nonribosomal peptides. Epimerization domains, embedded in nonribosomal peptide synthetases assembly lines, catalyze the l- to d-amino acid conversion. Here we report the structure of the epimerization domain/peptidyl carrier protein didomain construct from the first module of the cyclic peptide antibiotic gramicidin synthetase. Both holo (phosphopantethiene post-translationally modified) and apo structures were determined, each representing catalytically relevant conformations of the two domains. The structures provide insight into domain-domain recognition, substrate delivery during the assembly line process, in addition to the structural organization of homologous condensation domains, canonical players in all synthetase modules.

Interdomain and Intermodule Organization in Epimerization Domain Containing Nonribosomal Peptide Synthetases.,Chen WH, Li K, Guntaka NS, Bruner SD ACS Chem Biol. 2016 Jun 24. PMID:27294598<ref>PMID:27294598</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5isx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brevibacillus brevis]]
[[Category: Large Structures]]
[[Category: Bruner SD]]
[[Category: Chen W-H]]
[[Category: Li K]]