5isx: Difference between revisions
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New page: '''Unreleased structure''' The entry 5isx is ON HOLD until Paper Publication Authors: Chen, W.-H., Li, K., Bruner, S.D. Description: Category: Unreleased Structures [[Category: Li... |
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==Structure of the holo PCP-E didomain of the gramicidin S synthetase A== | |||
<StructureSection load='5isx' size='340' side='right'caption='[[5isx]], [[Resolution|resolution]] 2.33Å' 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]] 2.335Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5isx" style="background-color:#fffaf0;"></div> | ||
[[Category: Bruner | == References == | ||
[[Category: Chen | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevibacillus brevis]] | |||
[[Category: Large Structures]] | |||
[[Category: Bruner SD]] | |||
[[Category: Chen W-H]] | |||
[[Category: Li K]] | |||
Latest revision as of 14:08, 30 August 2023
Structure of the holo PCP-E didomain of the gramicidin S synthetase A
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