Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar

Dong Uk Kim, Ji Ho Yoo, Joo Lee Yong, Soo Kim Kwan, Hyun Soo Cho

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19 Citations (Scopus)


PM0188 is a newly identified sialyltransferase from P. multocida which transfers sialic acid from cytidine 5′-monophosphonuraminic acid (CMP-NeuAc) to an acceptor sugar. Although sialyltransferases are involved in important biological functions like cell-cell recognition, cell differentiation and receptor-ligand interactions, little is known about their catalytic mechanism. Here, we report the X-ray crystal structures of PM0188 in the presence of an acceptor sugar and a donor sugar analogue, revealing the precise mechanism of sialic acid transfer. Site-directed mutagenesis, kinetic assays, and structural analysis show that Asp141, His311, Glu338, Ser355 and Ser356 are important catalytic residues; Asp141 is especially crucial as it acts as a general base. These complex structures provide insights into the mechanism of sialyltransferases and the structure-based design of specific inhibitors.

Original languageEnglish
Pages (from-to)48-54
Number of pages7
JournalJournal of Biochemistry and Molecular Biology
Issue number1
Publication statusPublished - 2008 Jan 1


All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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