| Literature DB >> 10080886 |
M Hennig1, G E Dale, A D'arcy, F Danel, S Fischer, C P Gray, S Jolidon, F Müller, M G Page, P Pattison, C Oefner.
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. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID： 10080886 DOI： 10.1006/jmbi.1999.2623
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469