5AZI

Crystal structure of glycerol kinase from Trypanosoma brucei gambiense complexed with 4NP

Summary for 5AZI

• Entry DOI: 10.2210/pdb5azi/pdb
• Related: 3WXI 5AZJ
• Descriptor: Glycerol kinase, 4-NITROPHENYL PHOSPHATE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: glycerol kinase, phosphatase, 4np, african trypanosomes, transferase
• Biological source: Trypanosoma brucei gambiense; More
• Total number of polymer chains: 4
• Total formula weight: 229225.02

Authors

Balogun, E.O.,Inaoka, D.K.,Shiba, T.,Tokuoka, S.M.,Tokumasu, F.,Sakamoto, K.,Michels, P.A.M.,Harada, S.,Kita, K. (deposition date: 2015-10-08, release date: 2016-10-19, Last modification date: 2024-10-23)

Primary citation

Balogun, E.O.,Inaoka, D.K.,Shiba, T.,Tokuoka, S.M.,Tokumasu, F.,Sakamoto, K.,Kido, Y.,Michels, P.A.M.,Watanabe, Y.I.,Harada, S.,Kita, K.
Glycerol kinase of African trypanosomes possesses an intrinsic phosphatase activity.
Biochim Biophys Acta Gen Subj, 1861:2830-2842, 2017

PubMed Abstract: In general, glycerol kinases (GKs) are transferases that catalyze phospho group transfer from ATP to glycerol, and the mechanism was suggested to be random bi-bi. The reverse reaction i.e. phospho transfer from glycerol 3-phosphate (G3P) to ADP is only physiologically feasible by the African trypanosome GK. In contrast to other GKs the mechanism of Trypanosoma brucei gambiense glycerol kinase (TbgGK) was shown to be in an ordered fashion, and proceeding via autophosphorylation. From the unique reaction mechanism of TbgGK, we envisaged its potential to possess phosphatase activity in addition to being a kinase.

PubMed: 28778484
DOI: 10.1016/j.bbagen.2017.07.028

Experimental method

X-RAY DIFFRACTION (2.45 Å)