7TYB
Salicylate Adenylate PchD from Pseudomonas aeruginosa containing salicyl-AMS
Summary for 7TYB
| Entry DOI | 10.2210/pdb7tyb/pdb |
| Descriptor | Pyochelin biosynthesis protein PchD, 5'-O-[(2-hydroxybenzoyl)sulfamoyl]adenosine (3 entities in total) |
| Functional Keywords | siderophore, biosynthetic protein |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 60448.76 |
| Authors | Meneely, K.M.,Shelton, C.L.,Lamb, A.L. (deposition date: 2022-02-11, release date: 2022-05-18, Last modification date: 2023-10-18) |
| Primary citation | Shelton, C.L.,Meneely, K.M.,Ronnebaum, T.A.,Chilton, A.S.,Riley, A.P.,Prisinzano, T.E.,Lamb, A.L. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. J.Biol.Inorg.Chem., 27:541-551, 2022 Cited by PubMed Abstract: Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5'-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii. PubMed: 35513576DOI: 10.1007/s00775-022-01941-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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