6uly

Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P212121

spinqualitylabelsall models 6uly, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6uly is a 2 chain structure with sequence from Bacillus stratosphericus LAMA 585. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: GOL, QA7, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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.

Proteopedia Page Contributors and Editors (what is this?)

OCA