PDBsum entry 1zui

Transferase

PDB id: 1zui

Contents

Protein chain

158 a.a. *

Ligands

PO4

SKM

Waters ×66

* Residue conservation analysis

PDB id:

1zui

Name:

Transferase

Title:

Structural basis for shikimate-binding specificity of helicobacter pylori shikimate kinase

Structure:

Shikimate kinase. Chain: a. Engineered: yes

Source:

Helicobacter pylori. Organism_taxid: 85962. Strain: 26695. Gene: arok. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.207 R-free: 0.280

Authors:

W.C.Cheng,Y.N.Chang,W.C.Wang

Key ref:

W.C.Cheng et al. (2005). Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase. J Bacteriol, 187, 8156-8163. PubMed id: 16291688

Date:

31-May-05 Release date: 31-May-06

Protein chain

P56073  (AROK_HELPY) -  Shikimate kinase from Helicobacter pylori (strain ATCC 700392 / 26695)

Seq: 162 a.a.

Struc: 158 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.1.71 - shikimate kinase.
• Pathway: Shikimate and Chorismate Biosynthesis
• Reaction: shikimate + ATP = 3-phosphoshikimate + ADP + H⁺

shikimate + ATP (Bound ligand (Het Group name = SKM) corresponds exactly) = 3-phosphoshikimate + ADP + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Bacteriol 187:8156-8163 (2005)

PubMed id: 16291688

Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase.

W.C.Cheng, Y.N.Chang, W.C.Wang.

ABSTRACT

Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP. As the fifth key step in the shikimate pathway for aromatic amino acid biosynthesis in bacteria, fungi, and plants, but not mammals, shikimate kinase represents an attractive target for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here, we report the 1.8-Angstroms crystal structure of Helicobacter pylori shikimate kinase (HpSK). The crystal structure shows a three-layer alpha/beta fold consisting of a central sheet of five parallel beta-strands flanked by seven alpha-helices. An HpSK-shikimate-PO(4) complex was also determined and refined to 2.3 Angstroms, revealing induced-fit movement from an open to a closed form on substrate binding. Shikimate is located above a short 3(10) helix formed by a strictly conserved motif (GGGXV) after beta(3). Moreover, several highly conserved charged residues including Asp33 (in a conserved DT/SD motif), Arg57, and Arg132 (interacting with shikimate) are identified, guiding the development of novel inhibitors of shikimate kinase.