6ULZ

Adenylation domain of the initiation module of LgrA mutant P483M

Summary for 6ULZ

Entry DOI	10.2210/pdb6ulz/pdb
Descriptor	Linear gramicidin synthase subunit A, FORMIC ACID, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (5 entities in total)
Functional Keywords	nrps, nonribosomal peptide synthetase, non-ribosomal peptide synthetase, adenylation, adenylation domain, natural product, adenylate, biosynthetic protein
Biological source	Brevibacillus parabrevis
Total number of polymer chains	1
Total formula weight	78504.89
Authors	Chiche-Lapierre, C.,Alonzo, D.A.,Schmeing, T.M. (deposition date: 2019-10-08, release date: 2020-02-19, Last modification date: 2023-10-11)
Primary citation	Alonzo, D.A.,Chiche-Lapierre, C.,Tarry, M.J.,Wang, J.,Schmeing, T.M. Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis. Nat.Chem.Biol., 16:493-496, 2020 Cited by PubMed Abstract: Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from α-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for α-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoA' domain, structurally important for the depsipeptide module's synthetic cycle. PubMed: 32066969 DOI: 10.1038/s41589-020-0481-5 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.1 Å)

Structure validation