PDBsum entry: 1dgm

Transferase

PDB id: 1dgm

Contents

Protein chain

346 a.a. *

Ligands

ADN

ACY

Metals

_MG

_CL

Waters ×142

* Residue conservation analysis

PDB id:

1dgm

Name:

Transferase

Title:

Crystal structure of adenosine kinase from toxoplasma gondii

Structure:

Adenosine kinase. Chain: a. Engineered: yes. Mutation: yes

Source:

Toxoplasma gondii. Organism_taxid: 5811. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.214 R-free: 0.233

Authors:

W.J.Cook,L.J.Delucas,D.Chattopadhyay

Key ref:

W.J.Cook et al. (2000). Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution. Protein Sci, 9, 704-712. PubMed id: 10794412 Ref: Full text

Date:

24-Nov-99 Release date: 29-Nov-00

Protein chain

Q9TVW2  (ADK_TOXGO) -  Adenosine kinase

Seq: 363 a.a.

Struc: 346 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.1.20 - Adenosine kinase.
• Reaction: ATP + adenosine = ADP + AMP

ATP + adenosine (Bound ligand (Het Group name = ADN) corresponds exactly) = ADP + AMP

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

 Gene Ontology (GO) functional annotation 

• Biological process: purine ribonucleoside salvage (1 term)
• Biochemical function: nucleotide binding (6 terms)

reference

Full text	Protein Sci 9:704-712 (2000)
PubMed id: 10794412

Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.

W.J.Cook, L.J.DeLucas, D.Chattopadhyay.

ABSTRACT

Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme.