3RG2: Structure Of A Two-domain Nrps Fusion Protein Containing The Ente Adenylation Domain And Entb Aryl-carrier Protein From Enterobactin Biosynthesis

Nonribosomal peptide synthetases (NRPSs) are modular proteins that produce peptide antibiotics and siderophores. These enzymes act as catalytic assembly lines where substrates, covalently bound to integrated carrier domains, are delivered to adjacent catalytic domains. The carrier domains are initially loaded by adenylation domains, which use two distinct conformations to catalyze sequentially the adenylation of the substrate and the thioesterification of the pantetheine cofactor. We have used a mechanism-based inhibitor to determine the crystal structure of an engineered adenylation-carrier domain protein illustrating the intermolecular interaction between the adenylation and carrier domains. This structure enabled directed mutations to improve the interaction between nonnative partner proteins. Comparison with prior NRPS adenylation domain structures provides insights into the assembly line dynamics of these modular enzymes.
PDB ID: 3RG2Download
MMDB ID: 97750
PDB Deposition Date: 2011/4/7
Updated in MMDB: 2017/08
Experimental Method:
x-ray diffraction
Resolution: 3.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3RG2: dimeric; determined by author and by software (PISA)
Molecular Components in 3RG2
Label Count Molecule
Proteins (2 molecules)
Enterobactin Synthase Component E (Ente), 2,3-dihydro-2,3- Dihydroxybenzoate Synthetase, Isochroismatase (Entb)(Gene symbol: entE)
Molecule annotation
Chemicals (20 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB