2FQ1

Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains

Summary for 2FQ1

• Entry DOI: 10.2210/pdb2fq1/pdb
• Descriptor: Isochorismatase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: entb, nrps, multi-domain, acp, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 65902.46

Authors

Drake, E.J.,Nicolai, D.A.,Gulick, A.M. (deposition date: 2006-01-17, release date: 2006-05-02, Last modification date: 2023-08-30)

Primary citation

Drake, E.J.,Nicolai, D.A.,Gulick, A.M.
Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain.
Chem.Biol., 13:409-419, 2006

PubMed Abstract: Nonribosomal peptide synthetases are modular proteins that operate in an assembly line fashion to bind, modify, and link amino acids. In the E. coli enterobactin NRPS system, the EntE adenylation domain catalyzes the transfer of a molecule of 2,3-dihydroxybenzoic acid to the pantetheine cofactor of EntB. We present here the crystal structure of the EntB protein that contains an N-terminal isochorismate lyase domain that functions in the synthesis of 2,3-dihydroxybenzoate and a C-terminal carrier protein domain. Functional analysis showed that the EntB-EntE interaction was surprisingly tolerant of a number of point mutations on the surface of EntB and EntE. Mutational studies on EntE support our previous hypothesis that members of the adenylate-forming family of enzymes adopt two distinct conformations to catalyze the two-step reactions.

PubMed: 16632253
DOI: 10.1016/j.chembiol.2006.02.005

Experimental method

X-RAY DIFFRACTION (2.3 Å)