3W8R

Mutant structure of Thermus thermophilus HB8 uridine-cytidine kinase

Summary for 3W8R

• Entry DOI: 10.2210/pdb3w8r/pdb
• Related: 3ASY 3ASZ 3W34
• Descriptor: Uridine kinase, 4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: kinase, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 48866.24

Authors

Tomoike, F.,Nakagawa, N.,Masui, R.,Kuramitsu, S. (deposition date: 2013-03-21, release date: 2014-03-26, Last modification date: 2024-03-20)

Primary citation

Tomoike, F.,Nakagawa, N.,Fukui, K.,Yano, T.,Kuramitsu, S.,Masui, R.
Indispensable residue for uridine binding in the uridine-cytidine kinase family.
Biochem Biophys Rep, 11:93-98, 2017

PubMed Abstract: Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mechanism remains unresolved. Exhaustive mutagenesis of Tyr93 in ttCK revealed that the uridine phosphorylation activity was restored only by replacement of Tyr93 with His or Gln. Replacement of His117 in human UCK2, corresponding to residue Tyr93 in ttCK, by Tyr resulted in a loss of uridine phosphorylation activity. These findings indicated that uridine phosphorylation activity commonly depends on a single residue in the UCK family.

PubMed: 28955773
DOI: 10.1016/j.bbrep.2017.07.002

Experimental method

X-RAY DIFFRACTION (2.5 Å)