1Q0N

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM E. COLI WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.25 ANGSTROM RESOLUTION

Replaces:  1EQO

Summary for 1Q0N

• Entry DOI: 10.2210/pdb1q0n/pdb
• Related: 1CBK 1DY3 1EQ0 1EQM 1EQO 1EX8 1F9H 1F9Y 1G4C 1HKA 1HQ2 1IM6 1KBR
• Descriptor: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: pyrophosphokinase, pyrophosphoryl transfer, folate, hppk, pterin, 6-hydroxymethyl-7, 8-dihydropterin, ternary complex, substrate specificity, antimicrobial agent, drug design, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 18987.16

Authors

Blaszczyk, J.,Ji, X. (deposition date: 2003-07-16, release date: 2003-08-26, Last modification date: 2023-08-30)

Primary citation

Blaszczyk, J.,Shi, G.,Yan, H.,Ji, X.
Catalytic Center Assembly of Hppk as Revealed by the Crystal Structure of a Ternary Complex at 1.25 A Resolution
Structure, 8:1049-1058, 2000

PubMed Abstract: Folates are essential for life. Unlike mammals, most microorganisms must synthesize folates de novo. 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, and therefore is an ideal target for developing novel antimicrobial agents. HPPK from Escherichia coli is a 158-residue thermostable protein that provides a convenient model system for mechanistic studies. Crystal structures have been reported for HPPK without bound ligand, containing an HP analog, and complexed with an HP analog, two Mg(2+) ions, and ATP.

PubMed: 11080626
DOI: 10.1016/S0969-2126(00)00502-5

Experimental method

X-RAY DIFFRACTION (1.25 Å)