1NHK

CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE SUBSTRATE AT 2.0 ANGSTROMS RESOLUTION

Summary for 1NHK

• Entry DOI: 10.2210/pdb1nhk/pdb
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Myxococcus xanthus
• Cellular location: Cytoplasm (By similarity): P15266
• Total number of polymer chains: 2
• Total formula weight: 32709.16

Authors

Strelkov, S.,Williams, R.L. (deposition date: 1994-12-09, release date: 1995-03-31, Last modification date: 2024-02-14)

Primary citation

Strelkov, S.V.,Perisic, O.,Webb, P.A.,Williams, R.L.
The 1.9 A crystal structure of a nucleoside diphosphate kinase complex with adenosine 3',5'-cyclic monophosphate: evidence for competitive inhibition.
J.Mol.Biol., 249:665-674, 1995

PubMed Abstract: The X-ray structure of Myxococcus xanthus nucleoside diphosphate (NDP) kinase complexed with adenosine 3',5'-cyclic monophosphate (cAMP) has been determined. The structure was solved by difference Fourier analysis. The refined structure has a crystallographic R-factor of 0.17 at 1.9 A resolution. The phosphoryl group and ribose moiety make extensive polar interactions with the protein, whereas the base interacts only with two hydrophobic residues. The comparison with the structure of the enzyme complex with the substrate adenosine diphosphate (ADP) reported earlier shows that cAMP and ADP interact similarly with the enzyme. The base of the cAMP is present in two conformations, syn and anti, with respect to the sugar. The syn conformer is dominant. Based on the effect of cAMP on phosphorylation of the human NDP kinase NM23, it had been proposed that cAMP might interact with NDP kinase in a manner distinct from other nucleotides. However, the structure of the M. xanthus NDP kinase/cAMP complex indicates that the nucleotide is a competitive inhibitor of the enzyme and occupies the usual nucleotide site. Kinetic assays of the NDP kinase activity in the presence of cAMP were done. Their results are consistent with a competitive character of the cAMP inhibition.

PubMed: 7783219
DOI: 10.1006/jmbi.1995.0327

Experimental method

X-RAY DIFFRACTION (1.9 Å)