2rhs
PheRS from Staphylococcus haemolyticus- rational protein engineering and inhibitor studiesPheRS from Staphylococcus haemolyticus- rational protein engineering and inhibitor studies
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn this article, we describe for the first time the high-resolution crystal structure of a phenylalanine tRNA synthetase from the pathogenic bacterium Staphylococcus haemolyticus. We demonstrate the subtle yet important structural differences between this enzyme and the previously described Thermus thermophilus ortholog. We also explain the structure-activity relationship of several recently reported inhibitors. The native enzyme crystals were of poor quality--they only diffracted X-rays to 3-5A resolution. Therefore, we have executed a rational surface mutagenesis strategy that has yielded crystals of this 2300-amino acid multidomain protein, diffracting to 2A or better. This methodology is discussed and contrasted with the more traditional domain truncation approach. Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.,Evdokimov AG, Mekel M, Hutchings K, Narasimhan L, Holler T, McGrath T, Beattie B, Fauman E, Yan C, Heaslet H, Walter R, Finzel B, Ohren J, McConnell P, Braden T, Sun F, Spessard C, Banotai C, Al-Kassim L, Ma W, Wengender P, Kole D, Garceau N, Toogood P, Liu J J Struct Biol. 2008 Apr;162(1):152-69. Epub 2007 Nov 13. PMID:18086534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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