5isx

Structure of the holo PCP-E didomain of the gramicidin S synthetase A

spinqualitylabelsall models 5isx, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5isx is a 2 chain structure with sequence from Brevibacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.335Å Ligands: GOL, PNS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GRSA_BREBE In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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