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KMID : 0624620080410010048
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BMB Reports
2008 Volume.41 No. 1 p.48 ~ p.54
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Structural analysis of sialyltransferase PM0188 from Pasteurella multocida complexed with donor analogue and acceptor sugar
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Kim Dong-Uk
Yoo Ji-Ho
Lee Yong-Joo
Kim Kwan-Soo
Cho Hyun-Soo
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Abstract
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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. [BMB reports 2008; 41(1): 48-54]
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KEYWORD
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CMP-3FNeuAc, CMP-NeuAc, Lactose, PM0188, Sialyltransferase, X-ray crystallography
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