1w7w
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1w7w.gif|left|200px]] | [[Image:1w7w.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1w7w", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1w7w| PDB=1w7w | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE AND MUTATIONAL ANALYSIS OF A PLANT MITOCHONDRIAL NUCLEOSIDE DIPHOSPHATE KINASE: IDENTIFICATION OF RESIDUES INVOLVED IN SERINE PHOSPHORYLATION AND OLIGOMERIZATION.''' | '''STRUCTURE AND MUTATIONAL ANALYSIS OF A PLANT MITOCHONDRIAL NUCLEOSIDE DIPHOSPHATE KINASE: IDENTIFICATION OF RESIDUES INVOLVED IN SERINE PHOSPHORYLATION AND OLIGOMERIZATION.''' | ||
| Line 30: | Line 27: | ||
[[Category: Knorpp, C.]] | [[Category: Knorpp, C.]] | ||
[[Category: Mackenzie-Hose, A.]] | [[Category: Mackenzie-Hose, A.]] | ||
| - | [[Category: | + | [[Category: Kinase]] |
| - | [[Category: | + | [[Category: Mitochondrial nucleoside diphosphate kinase]] |
| - | [[Category: | + | [[Category: Ndpk3]] |
| - | [[Category: | + | [[Category: Pisum sativum]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:16:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:16, 3 May 2008
STRUCTURE AND MUTATIONAL ANALYSIS OF A PLANT MITOCHONDRIAL NUCLEOSIDE DIPHOSPHATE KINASE: IDENTIFICATION OF RESIDUES INVOLVED IN SERINE PHOSPHORYLATION AND OLIGOMERIZATION.
Overview
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.
About this Structure
1W7W is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.
Reference
Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase. Identification of residues involved in serine phosphorylation and oligomerization., Johansson M, Mackenzie-Hose A, Andersson I, Knorpp C, Plant Physiol. 2004 Oct;136(2):3034-42. Epub 2004 Oct 1. PMID:15466238 Page seeded by OCA on Sat May 3 13:16:52 2008
