PDBsum entry 2zgi

Lyase

PDB id: 2zgi

Contents

Protein chains

244 a.a. *

Ligands

SO4 ×4

PLP ×4

PGE ×2

PEG ×3

Waters ×1318

* Residue conservation analysis

PDB id:

2zgi

Name:

Lyase

Title:

Crystal structure of putative 4-amino-4-deoxychorismate lyase

Structure:

Putative 4-amino-4-deoxychorismate lyase. Chain: a, b, c, d. Engineered: yes

Source:

Thermus thermophilus. Strain: hb8. Expressed in: escherichia coli.

Resolution:

1.93Å R-factor: 0.196 R-free: 0.249

Authors:

B.Padmanabhan,Y.Bessho,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

B.Padmanabhan et al. (2009). Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1234-1239. PubMed id: 20054118

Date:

22-Jan-08 Release date: 22-Jul-08

Protein chains

Q5SKM2  (Q5SKM2_THET8) -  4-amino-4-deoxychorismate lyase from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 246 a.a.

Struc: 244 a.a.

Enzyme reactions

• Enzyme class: E.C.4.-.-.-

Acta Crystallogr Sect F Struct Biol Cryst Commun 65:1234-1239 (2009)

PubMed id: 20054118

Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8.

B.Padmanabhan, Y.Bessho, A.Ebihara, S.V.Antonyuk, M.J.Ellis, R.W.Strange, S.Kuramitsu, N.Watanabe, S.S.Hasnain, S.Yokoyama.

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.