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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1999-4-28
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
pubmed-author:D'arcyAA,
pubmed-author:DaleG EGE,
pubmed-author:DanesAA,
pubmed-author:FischerSS,
pubmed-author:GrayC PCP,
pubmed-author:HennigMM,
pubmed-author:JolidonSS,
pubmed-author:MüllerFF,
pubmed-author:OefnerCC,
pubmed-author:PageM GMG,
pubmed-author:PattisonPP
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
287
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10080886-Adenosine Triphosphate,
pubmed-meshheading:10080886-Amino Acid Sequence,
pubmed-meshheading:10080886-Binding Sites,
pubmed-meshheading:10080886-Calorimetry, Differential Scanning,
pubmed-meshheading:10080886-Cloning, Molecular,
pubmed-meshheading:10080886-Crystallography, X-Ray,
pubmed-meshheading:10080886-Diphosphotransferases,
pubmed-meshheading:10080886-Enzyme Inhibitors,
pubmed-meshheading:10080886-Escherichia coli,
pubmed-meshheading:10080886-Haemophilus influenzae,
pubmed-meshheading:10080886-Models, Molecular,
pubmed-meshheading:10080886-Molecular Sequence Data,
pubmed-meshheading:10080886-Protein Conformation,
pubmed-meshheading:10080886-Protein Structure, Secondary,
pubmed-meshheading:10080886-Pterins,
pubmed-meshheading:10080886-Recombinant Proteins,
pubmed-meshheading:10080886-Selenomethionine,
pubmed-meshheading:10080886-Sequence Alignment,
pubmed-meshheading:10080886-Sequence Analysis, DNA,
pubmed-meshheading:10080886-Spectrometry, Fluorescence,
pubmed-meshheading:10080886-Ultracentrifugation
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pubmed:year |
1999
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pubmed:articleTitle |
The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae.
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pubmed:affiliation |
F. Hoffmann-La Roche Ltd, Pharma Preclinical Research, Basel, CH-4070, Switzerland.
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pubmed:publicationType |
Journal Article
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