1QR7

CRYSTAL STRUCTURE OF PHENYLALANINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM ESCHERICHIA COLI COMPLEXED WITH PB2+ AND PEP

Summary for 1QR7

Entry DOI	10.2210/pdb1qr7/pdb
Descriptor	PHENYLALANINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE, LEAD (II) ION, SULFATE ION, ... (5 entities in total)
Functional Keywords	beta-alpha-barrel, lyase
Biological source	Escherichia coli
Total number of polymer chains	4
Total formula weight	154123.24
Authors	Shumilin, I.A.,Kretsinger, R.H.,Bauerle, R.H. (deposition date: 1999-06-18, release date: 1999-08-31, Last modification date: 2024-02-14)
Primary citation	Shumilin, I.A.,Kretsinger, R.H.,Bauerle, R.H. Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure Fold.Des., 7:865-875, 1999 Cited by PubMed Abstract: In microorganisms and plants the first step in the common pathway leading to the biosynthesis of aromatic compounds is the stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). This reaction is catalyzed by DAHP synthase (DAHPS), a metal-activated enzyme, which in microorganisms is the target for negative-feedback regulation by pathway intermediates or by end products. In Escherichia coli there are three DAHPS isoforms, each specifically inhibited by one of the three aromatic amino acids. PubMed: 10425687 DOI: 10.1016/S0969-2126(99)80109-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation