Conformational flexibility influences structure–function relationships in tyrosyl protein sulfotransferase-2

Warispreet Singh, Tatyana Karabencheva-Christova, Gary Black, Olivier Sparagano, Christo Christov

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)
6 Downloads (Pure)


Tyrosine sulfation is a very important posttranslational modification of proteins. It is catalyzed by tyrosylprotein sulfotransferase and recently became increasingly important for biomedicine and pharmacy. An important insight about structure–activity relationships of human tyrosylprotein sulfotransferase has been received by elucidating the crystal structure, but there is still no understanding about how conformational flexibility and dynamics which are fundamental protein properties influence structure–function relationships of the enzyme. In order to provide this missing but crucially important knowledge we performed a comprehensive atomistic molecular dynamics study which revealed that (i) the conformational flexibility influences sensitively key structural determinants and interactions between the enzyme, the substrate and the cofactor; (ii) a more open conformation adopted by the substrate for binding in TPST 2; (iii) the mutations of key residues related with catalysis and binding change alter the enzyme structure and influence important interactions between the enzyme, the cofactor and the substrate.
Original languageEnglish
Pages (from-to)11344-11352
JournalRSC Advances
Issue number14
Early online date18 Jan 2016
Publication statusPublished - 2016


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