6mfy

Crystal structure of a 5-domain construct of LgrA in the substrate donation state

spinqualitylabelsall models 6mfy, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mfy is a 1 chain structure with sequence from Atcc 10027. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PNS, PO4 Gene: lgrA (ATCC 10027) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LGRA_BREPA] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide. Publication Abstract from PubMed Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes that synthesize natural product therapeutics using a modular synthetic logic, whereby each module adds one aminoacyl substrate to the nascent peptide. We have determined five x-ray crystal structures of large constructs of the NRPS linear gramicidin synthetase, including a structure of a full core dimodule in conformations organized for the condensation reaction and intermodular peptidyl substrate delivery. The structures reveal differences in the relative positions of adjacent modules, which are not strictly coupled to the catalytic cycle and are consistent with small-angle x-ray scattering data. The structures and covariation analysis of homologs allowed us to create mutants that improve the yield of a peptide from a module-swapped dimodular NRPS. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.,Reimer JM, Eivaskhani M, Harb I, Guarne A, Weigt M, Schmeing TM Science. 2019 Nov 8;366(6466). pii: 366/6466/eaaw4388. doi:, 10.1126/science.aaw4388. PMID:31699907 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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