2fq1

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spinqualitylabelsall models 2fq1, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2FQ1 is a Single protein structure of sequence from Escherichia coli with MG, CL and EDO as ligands. Active as Isochorismatase, with EC number 3.3.2.1 Full crystallographic information is available from OCA.

Reference

Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain., Drake EJ, Nicolai DA, Gulick AM, Chem Biol. 2006 Apr;13(4):409-19. PMID:16632253

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