1HHQ

Role of active site resiude Lys16 in Nucleoside Diphosphate Kinase

Summary for 1HHQ

• Entry DOI: 10.2210/pdb1hhq/pdb
• Related: 1B4S 1B99 1BUX 1F3F 1F6T 1HIY 1KDN 1LEO 1LWX 1NCL 1NPK 2BEF
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE, SULFATE ION (3 entities in total)
• Functional Keywords: metabolic role, transferase, kinase
• Biological source: DICTYOSTELIUM DISCOIDEUM
• Total number of polymer chains: 1
• Total formula weight: 16854.30

Authors

Schneider, B.,Babolat, M.,Xu, Y.W.,Janin, J.,Veron, M.,Deville-Bonne, D. (deposition date: 2000-12-26, release date: 2001-05-31, Last modification date: 2023-12-13)

Primary citation

Schneider, B.,Babolat, M.,Xu, Y.W.,Janin, J.,Veron, M.,Deville-Bonne, D.
Mechanism of Phosphoryl Transfer by Nucleoside Diphosphate Kinase Ph-Dependence and Role of Active Site Lys16 and Tyr56 Residues
Eur.J.Biochem., 268:1964-, 2001

PubMed Abstract: Nucleoside diphosphate (NDP) kinase phosphorylates nucleoside diphosphates with little specificity for the base and the sugar. Although nucleotide analogues used in antiviral therapies are also metabolized to their triphosphate form by NDP kinase, their lack of the 3'-hydroxyl of the ribose, which allows them to be DNA chain terminators, severely impairs the catalytic efficiency of NDP kinase. We have analyzed the kinetics parameters of several mutant NDP kinases modified on residues (Lys16, Tyr56, Asn119) interacting with the gamma-phosphate and/or the 3'-OH of the Mg2+-ATP substrate. We compared the relative contributions of the active-site residues and the substrate 3'-OH for point mutations on Lys16, Tyr56 and Asn119. Analysis of additional data from pH profiles identify the ionization state of these residues in the enzyme active form. X-ray structure of K16A mutant NDP kinase shows no detectable rearrangement of the residues of the active site.

PubMed: 11277918
DOI: 10.1046/J.1432-1327.2001.02070.X

Experimental method

X-RAY DIFFRACTION (2.1 Å)