PDBsum entry 2zgi

Lyase

PDB id: 2zgi

Contents

Protein chains

244 a.a.

Ligands

SO4 ×4

PLP ×4

PGE ×2

PEG ×3

Waters ×1318

References listed in PDB file

Key reference

• Title: Structure of putative 4-Amino-4-Deoxychorismate lyase from thermus thermophilus hb8.
• Authors: B.Padmanabhan, Y.Bessho, A.Ebihara, S.V.Antonyuk, M.J.Ellis, R.W.Strange, S.Kuramitsu, N.Watanabe, S.S.Hasnain, S.Yokoyama.
• Ref.: Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009, 65, 1234-1239.
• PubMed id: 20054118

Abstract

The pyridoxal 5'-phosphate-dependent enzyme 4-amino-4-deoxychorismate lyase converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate in one of the crucial steps in the folate-biosynthesis pathway. The primary structure of the hypothetical protein TTHA0621 from Thermus thermophilus HB8 suggests that TTHA0621 is a putative 4-amino-4-deoxychorismate lyase. Here, the crystal structure of TTHA0621 is reported at 1.93 A resolution. The asymmetric unit contained four NCS molecules related by 222 noncrystallographic symmetry, in which the formation of intact dimers may be functionally important. The cofactor pyridoxal 5'-phosphate (PLP) binds to the protein in the large cleft formed by the N-terminal and C-terminal domains of TTHA0621. The high structural similarity and the conservation of the functional residues in the catalytic region compared with 4-amino-4-deoxychorismate lyase (PabC; EC 4.1.3.38) from Escherichia coli suggest that the TTHA0621 protein may also possess 4-amino-4-deoxychorismate lyase activity.