PDBsum entry: 1w7w

Transferase

PDB id: 1w7w

Contents

Protein chains

(+ 0 more) 151 a.a. *

Waters ×54

* Residue conservation analysis

PDB id:

1w7w

Name:

Transferase

Title:

Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase: identification of residues involved in serine phosphorylation and oligomerization.

Structure:

Nucleoside diphosphate kinase. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Pisum sativum. Pea. Organism_taxid: 3888. Strain: oregon sugar pod. Expressed in: esherichia coli.

Biol. unit:

Hexamer (from PDB file)

Resolution:

2.80Å R-factor: 0.237 R-free: 0.264

Authors:

M.Johansson,A.Mackenzie-Hose,I.Andersson,C.Knorpp

Key ref:

M.Johansson et al. (2004). Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase. Identification of residues involved in serine phosphorylation and oligomerization. Plant Physiol, 136, 3034-3042. PubMed id: 15466238 DOI: 10.1104/pp.104.044040

Date:

13-Sep-04 Release date: 22-Oct-04

Protein chains

Q9SP13  (Q9SP13_PEA) -  Nucleoside diphosphate kinase

Seq: 233 a.a.

Struc: 151 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.4.6 - Nucleoside-diphosphate kinase.
• Reaction: ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

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

 Gene Ontology (GO) functional annotation 

• Biological process: GTP biosynthetic process (3 terms)
• Biochemical function: nucleoside diphosphate kinase activity (2 terms)

reference

DOI no: 10.1104/pp.104.044040

Plant Physiol 136:3034-3042 (2004)

PubMed id: 15466238

Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase. Identification of residues involved in serine phosphorylation and oligomerization.

M.Johansson, A.Mackenzie-Hose, I.Andersson, C.Knorpp.

ABSTRACT

We report the first crystal structure of a plant (Pisum sativum L. cv Oregon sugarpod) mitochondrial nucleoside diphosphate kinase. Similar to other eukaryotic nucleoside diphosphate kinases, the plant enzyme is a hexamer; the six monomers in the asymmetric unit are arranged as trimers of dimers. Different functions of the kinase have been correlated with the oligomeric structure and the phosphorylation of Ser residues. We show that the occurrence of Ser autophosphorylation depends on enzymatic activity. The mutation of the strictly conserved Ser-119 to Ala reduced the Ser phosphorylation to about one-half of that observed in wild type with only a modest change of enzyme activity. We also show that mutating another strictly conserved Ser, Ser-69, to Ala reduces the enzyme activity to 6% and 14% of wild-type using dCDP and dTDP as acceptors, respectively. Changes in the oligomerization pattern of the S69A mutant were observed by cross-linking experiments. A reduction in trimer formation and a change in the dimer interaction could be detected with a concomitant increase of tetramers. We conclude that the S69 mutant is involved in the stabilization of the oligomeric state of this plant nucleoside diphosphate kinase.