1CBK

7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE

Summary for 1CBK

• Entry DOI: 10.2210/pdb1cbk/pdb
• Descriptor: PROTEIN (7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE), SULFATE ION, 7,8-DIHYDRO-7,7-DIMETHYL-6-HYDROXYPTERIN, ... (4 entities in total)
• Functional Keywords: pyrophosphokinase, transferase
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 2
• Total formula weight: 37250.56

Authors

Hennig, M.,D'Arcy, A.,Dale, G.,Oefner, C. (deposition date: 1999-02-26, release date: 2000-03-01, Last modification date: 2023-12-27)

Primary citation

Hennig, M.,Dale, G.E.,D'arcy, A.,Danel, F.,Fischer, S.,Gray, C.P.,Jolidon, S.,Muller, F.,Page, M.G.,Pattison, P.,Oefner, C.
The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae.
J.Mol.Biol., 287:211-219, 1999

PubMed Abstract: The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices and on the other by three consecutive alpha-helices, giving a novel beta1alpha1beta2beta3alpha2beta4alpha3alpha4alpha5 polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 A resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme.

PubMed: 10080886
DOI: 10.1006/jmbi.1999.2623

Experimental method

X-RAY DIFFRACTION (2.02 Å)