Motion in 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase [hppk]

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Classification [D-h-2]

Structures
1HKA
1EQO

Description
6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK), catalyzes pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate pathway. This motion represents the movement of HPPK when in complex with HP, two Mg2+ ions, and AMPCPP (an ATP analog that inhibits the enzymatic reaction). The enzyme seals the active center where the reaction occurs. The comparison with unligated HPPK reveals dramatic conformational changes of three flexible loops and many sidechains.

References
T L Talarico, P H Ray, I K Dev, B M Merrill, W S Dallas (1992). Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. J Bacteriol, 174:5971-7 [Medline info for 1325970]
B Xiao, G Shi, X Chen, H Yan, X Ji (1999). Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure Fold Des, 7:489-96 [Medline info for 10378268]
T L Talarico, I K Dev, W S Dallas, R Ferone, P H Ray (1991). Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100. J Bacteriol, 173:7029-32 [Medline info for 1657875]
J Blaszczyk, G Shi, H Yan, X Ji (2000). Catalytic center assembly of HPPK as revealed by the crystal structure of a ternary complex at 1.25 A resolution. Structure Fold Des, 8:1049-58 [Medline info for 11080626]

GO terms associated with structures
Molecular function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
Biological processfolic acid and derivative biosynthesis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu