6ulz

Adenylation domain of the initiation module of LgrA mutant P483MAdenylation domain of the initiation module of LgrA mutant P483M

Structural highlights 6ulz is a 1 chain structure with sequence from Brevibacillus parabrevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: , , 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 depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from alpha-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for alpha-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle. Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis.,Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM Nat Chem Biol. 2020 Feb 17. pii: 10.1038/s41589-020-0481-5. doi:, 10.1038/s41589-020-0481-5. PMID:32066969 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Linear gramicidin synthase

spinqualitylabelsall models 6ulz, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image